GenomeNet

Database: UniProt/TrEMBL
Entry: F9P8F1_STRCV X8H6L1_9STRE F5U0M7_STRAP U2Y3K4_STRIT I0SF24_STRCV J5H093_STRAP T1ZWM4_STRAP E6J202_STRAP I0SE83_STRAP A0A0C1K7P6_STRCV G6A2V0_STRIT U2ZUC7_STRAP
LinkDB: F9P8F1_STRCV X8H6L1_9STRE F5U0M7_STRAP U2Y3K4_STRIT I0SF24_STRCV J5H093_STRAP T1ZWM4_STRAP E6J202_STRAP I0SE83_STRAP A0A0C1K7P6_STRCV G6A2V0_STRIT U2ZUC7_STRAP
Original site: F9P8F1_STRCV X8H6L1_9STRE F5U0M7_STRAP U2Y3K4_STRIT I0SF24_STRCV J5H093_STRAP T1ZWM4_STRAP E6J202_STRAP I0SE83_STRAP A0A0C1K7P6_STRCV G6A2V0_STRIT U2ZUC7_STRAP 
tr:F5U0M7_STRAP : No such data.
tr:U2Y3K4_STRIT : No such data.
tr:I0SF24_STRCV : No such data.
tr:J5H093_STRAP : No such data.
tr:T1ZWM4_STRAP : No such data.
tr:G6A2V0_STRIT : No such data.

ID   F9P8F1_STRCV            Unreviewed;       398 AA.
AC   F9P8F1;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Elongation factor Tu {ECO:0000256|ARBA:ARBA00029554, ECO:0000256|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118};
GN   ORFNames=ANG5_0815 {ECO:0000313|EMBL:GAD44287.1}, HMPREF1042_1506
GN   {ECO:0000313|EMBL:EGV08383.1};
OS   Streptococcus constellatus subsp. pharyngis SK1060 = CCUG 46377.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus; Streptococcus anginosus group.
OX   NCBI_TaxID=1035184 {ECO:0000313|EMBL:EGV08383.1, ECO:0000313|Proteomes:UP000003287};
RN   [1] {ECO:0000313|EMBL:EGV08383.1, ECO:0000313|Proteomes:UP000003287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK1060 {ECO:0000313|EMBL:EGV08383.1,
RC   ECO:0000313|Proteomes:UP000003287};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Nelson K.E.;
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAD44287.1, ECO:0000313|Proteomes:UP000016985}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 46377 {ECO:0000313|EMBL:GAD44287.1}, and CCUG46377
RC   {ECO:0000313|Proteomes:UP000016985};
RA   Maruyama F., Sakurai A., Ogura Y., Homma H., Takahashi N., Ohtsubo Y.,
RA   Hoshino T., Okahashi N., Nakagawa I., Kimura S., Fujiwara T., Hayashi T.,
RA   Shintani S.;
RT   "Genome Sequences of seven clinical isolates and type strains of anginosus
RT   group streptococci.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000256|ARBA:ARBA00007249, ECO:0000256|HAMAP-
CC       Rule:MF_00118}.
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DR   EMBL; AFUP01000004; EGV08383.1; -; Genomic_DNA.
DR   EMBL; BASX01000005; GAD44287.1; -; Genomic_DNA.
DR   RefSeq; WP_003023932.1; NZ_BASX01000005.1.
DR   AlphaFoldDB; F9P8F1; -.
DR   GeneID; 58100039; -.
DR   eggNOG; COG0050; Bacteria.
DR   Proteomes; UP000003287; Unassembled WGS sequence.
DR   Proteomes; UP000016985; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01884; EF_Tu; 1.
DR   CDD; cd03697; EFTU_II; 1.
DR   CDD; cd03707; EFTU_III; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
DR   InterPro; IPR041709; EF-Tu_GTP-bd.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR033720; EFTU_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   NCBIfam; TIGR00485; EF-Tu; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00118}.
FT   DOMAIN          10..207
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT   BINDING         84..88
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT   BINDING         139..142
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   398 AA;  44063 MW;  CB4843FE231D0CD9 CRC64;
     MAKEKYDRSK PHVNIGTIGH VDHGKTTLTA AITTVLARRL PSSVNQPKDY SSIDAAPEER
     ERGITINTAH VEYETAKRHY AHIDAPGHAD YVKNMITGAA QMDGAILVVA STDGPMPQTR
     EHILLSRQVG VKYLIVFMNK VDLVDDEELL ELVEMEIRDL LSEYDFPGDE IPVIQGSALK
     ALEGDEKYED IIMELMDTVD EYIPEPERDT DKPLLLPVED VFSITGRGTV ASGRIDRGTV
     KVNDEVEIVG IRDEIQKAVV TGVEMFRKQL DEGLAGDNVG VLLRGIQRDE IERGQVLAKP
     GSIHPHTKFK GEVYILTKEE GGRHTPFFNN YRPQFYFRTT DVTGSIELPA GTEMVMPGDN
     VTIDVELIHP IAVEQGTTFS IREGGRTVGS GMVTEIEA
//
ID   X8H6L1_9STRE            Unreviewed;       398 AA.
AC   X8H6L1;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Elongation factor Tu {ECO:0000256|ARBA:ARBA00029554, ECO:0000256|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118,
GN   ECO:0000313|EMBL:EUB23225.1};
GN   ORFNames=HMPREF1514_0384 {ECO:0000313|EMBL:EUB23225.1};
OS   Streptococcus sp. AS20.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=936578 {ECO:0000313|EMBL:EUB23225.1, ECO:0000313|Proteomes:UP000022711};
RN   [1] {ECO:0000313|EMBL:EUB23225.1, ECO:0000313|Proteomes:UP000022711}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AS20 {ECO:0000313|EMBL:EUB23225.1,
RC   ECO:0000313|Proteomes:UP000022711};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Haft D.H., Methe B.,
RA   Sutton G., Nelson K.E.;
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000256|ARBA:ARBA00007249, ECO:0000256|HAMAP-
CC       Rule:MF_00118}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EUB23225.1}.
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DR   EMBL; JANS01000013; EUB23225.1; -; Genomic_DNA.
DR   RefSeq; WP_003023932.1; NZ_JANS01000013.1.
DR   AlphaFoldDB; X8H6L1; -.
DR   GeneID; 58100039; -.
DR   PATRIC; fig|936578.3.peg.1656; -.
DR   Proteomes; UP000022711; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01884; EF_Tu; 1.
DR   CDD; cd03697; EFTU_II; 1.
DR   CDD; cd03707; EFTU_III; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
DR   InterPro; IPR041709; EF-Tu_GTP-bd.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR033720; EFTU_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   NCBIfam; TIGR00485; EF-Tu; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00118}.
FT   DOMAIN          10..207
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT   BINDING         84..88
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT   BINDING         139..142
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   398 AA;  44063 MW;  CB4843FE231D0CD9 CRC64;
     MAKEKYDRSK PHVNIGTIGH VDHGKTTLTA AITTVLARRL PSSVNQPKDY SSIDAAPEER
     ERGITINTAH VEYETAKRHY AHIDAPGHAD YVKNMITGAA QMDGAILVVA STDGPMPQTR
     EHILLSRQVG VKYLIVFMNK VDLVDDEELL ELVEMEIRDL LSEYDFPGDE IPVIQGSALK
     ALEGDEKYED IIMELMDTVD EYIPEPERDT DKPLLLPVED VFSITGRGTV ASGRIDRGTV
     KVNDEVEIVG IRDEIQKAVV TGVEMFRKQL DEGLAGDNVG VLLRGIQRDE IERGQVLAKP
     GSIHPHTKFK GEVYILTKEE GGRHTPFFNN YRPQFYFRTT DVTGSIELPA GTEMVMPGDN
     VTIDVELIHP IAVEQGTTFS IREGGRTVGS GMVTEIEA
//
ID   E6J202_STRAP            Unreviewed;       398 AA.
AC   E6J202;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=Elongation factor Tu {ECO:0000256|ARBA:ARBA00029554, ECO:0000256|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118,
GN   ECO:0000313|EMBL:EFU21938.1};
GN   ORFNames=HMPREF0813_01290 {ECO:0000313|EMBL:EFU21938.1};
OS   Streptococcus anginosus F0211.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus; Streptococcus anginosus group.
OX   NCBI_TaxID=706437 {ECO:0000313|EMBL:EFU21938.1, ECO:0000313|Proteomes:UP000002973};
RN   [1] {ECO:0000313|EMBL:EFU21938.1, ECO:0000313|Proteomes:UP000002973}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0211 {ECO:0000313|EMBL:EFU21938.1,
RC   ECO:0000313|Proteomes:UP000002973};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000256|ARBA:ARBA00007249, ECO:0000256|HAMAP-
CC       Rule:MF_00118}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFU21938.1}.
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DR   EMBL; AECT01000035; EFU21938.1; -; Genomic_DNA.
DR   RefSeq; WP_003023932.1; NZ_AECT01000035.1.
DR   AlphaFoldDB; E6J202; -.
DR   GeneID; 58100039; -.
DR   eggNOG; COG0050; Bacteria.
DR   Proteomes; UP000002973; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01884; EF_Tu; 1.
DR   CDD; cd03697; EFTU_II; 1.
DR   CDD; cd03707; EFTU_III; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
DR   InterPro; IPR041709; EF-Tu_GTP-bd.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR033720; EFTU_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   NCBIfam; TIGR00485; EF-Tu; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00118}.
FT   DOMAIN          10..207
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT   BINDING         84..88
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT   BINDING         139..142
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   398 AA;  44063 MW;  CB4843FE231D0CD9 CRC64;
     MAKEKYDRSK PHVNIGTIGH VDHGKTTLTA AITTVLARRL PSSVNQPKDY SSIDAAPEER
     ERGITINTAH VEYETAKRHY AHIDAPGHAD YVKNMITGAA QMDGAILVVA STDGPMPQTR
     EHILLSRQVG VKYLIVFMNK VDLVDDEELL ELVEMEIRDL LSEYDFPGDE IPVIQGSALK
     ALEGDEKYED IIMELMDTVD EYIPEPERDT DKPLLLPVED VFSITGRGTV ASGRIDRGTV
     KVNDEVEIVG IRDEIQKAVV TGVEMFRKQL DEGLAGDNVG VLLRGIQRDE IERGQVLAKP
     GSIHPHTKFK GEVYILTKEE GGRHTPFFNN YRPQFYFRTT DVTGSIELPA GTEMVMPGDN
     VTIDVELIHP IAVEQGTTFS IREGGRTVGS GMVTEIEA
//
ID   I0SE83_STRAP            Unreviewed;       398 AA.
AC   I0SE83;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Elongation factor Tu {ECO:0000256|ARBA:ARBA00029554, ECO:0000256|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118,
GN   ECO:0000313|EMBL:EID21686.1};
GN   ORFNames=HMPREF1043_1406 {ECO:0000313|EMBL:EID21686.1};
OS   Streptococcus anginosus subsp. whileyi CCUG 39159.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus; Streptococcus anginosus group.
OX   NCBI_TaxID=1095729 {ECO:0000313|EMBL:EID21686.1, ECO:0000313|Proteomes:UP000003245};
RN   [1] {ECO:0000313|EMBL:EID21686.1, ECO:0000313|Proteomes:UP000003245}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 39159 {ECO:0000313|EMBL:EID21686.1,
RC   ECO:0000313|Proteomes:UP000003245};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Nelson K.E.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000256|ARBA:ARBA00007249, ECO:0000256|HAMAP-
CC       Rule:MF_00118}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EID21686.1}.
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DR   EMBL; AICP01000040; EID21686.1; -; Genomic_DNA.
DR   RefSeq; WP_003023932.1; NZ_AICP01000040.1.
DR   AlphaFoldDB; I0SE83; -.
DR   GeneID; 58100039; -.
DR   PATRIC; fig|1095729.3.peg.1184; -.
DR   Proteomes; UP000003245; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01884; EF_Tu; 1.
DR   CDD; cd03697; EFTU_II; 1.
DR   CDD; cd03707; EFTU_III; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
DR   InterPro; IPR041709; EF-Tu_GTP-bd.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR033720; EFTU_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   NCBIfam; TIGR00485; EF-Tu; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00118}.
FT   DOMAIN          10..207
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT   BINDING         84..88
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT   BINDING         139..142
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   398 AA;  44063 MW;  CB4843FE231D0CD9 CRC64;
     MAKEKYDRSK PHVNIGTIGH VDHGKTTLTA AITTVLARRL PSSVNQPKDY SSIDAAPEER
     ERGITINTAH VEYETAKRHY AHIDAPGHAD YVKNMITGAA QMDGAILVVA STDGPMPQTR
     EHILLSRQVG VKYLIVFMNK VDLVDDEELL ELVEMEIRDL LSEYDFPGDE IPVIQGSALK
     ALEGDEKYED IIMELMDTVD EYIPEPERDT DKPLLLPVED VFSITGRGTV ASGRIDRGTV
     KVNDEVEIVG IRDEIQKAVV TGVEMFRKQL DEGLAGDNVG VLLRGIQRDE IERGQVLAKP
     GSIHPHTKFK GEVYILTKEE GGRHTPFFNN YRPQFYFRTT DVTGSIELPA GTEMVMPGDN
     VTIDVELIHP IAVEQGTTFS IREGGRTVGS GMVTEIEA
//
ID   A0A0C1K7P6_STRCV        Unreviewed;       398 AA.
AC   A0A0C1K7P6;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Elongation factor Tu {ECO:0000256|ARBA:ARBA00029554, ECO:0000256|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118,
GN   ECO:0000313|EMBL:KIC78886.1};
GN   ORFNames=DYJ42_05935 {ECO:0000313|EMBL:RID96179.1}, I6J38_04485
GN   {ECO:0000313|EMBL:QRP82520.1}, NCTC11325_01240
GN   {ECO:0000313|EMBL:SUN40845.1}, RN79_04785
GN   {ECO:0000313|EMBL:KIC78886.1}, SCODD09_00213
GN   {ECO:0000313|EMBL:KXU02771.1};
OS   Streptococcus constellatus.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus; Streptococcus anginosus group.
OX   NCBI_TaxID=76860 {ECO:0000313|EMBL:KIC78886.1, ECO:0000313|Proteomes:UP000031339};
RN   [1] {ECO:0000313|EMBL:KIC78886.1, ECO:0000313|Proteomes:UP000031339}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCOM 1650 {ECO:0000313|EMBL:KIC78886.1,
RC   ECO:0000313|Proteomes:UP000031339};
RA   Kook J.-K., Park S.-N., Lim Y.K., Jo E.;
RT   "Partial genome sequence of Streptococcus constellatus KCOM 1650 (= ChDC
RT   B144).";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KXU02771.1, ECO:0000313|Proteomes:UP000073019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD09 {ECO:0000313|EMBL:KXU02771.1,
RC   ECO:0000313|Proteomes:UP000073019};
RA   Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I.,
RA   Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.;
RT   "Highly variable Streptococcus oralis are common among viridans
RT   streptococci isolated from primates.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SUN40845.1, ECO:0000313|Proteomes:UP000254426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC11325 {ECO:0000313|EMBL:SUN40845.1,
RC   ECO:0000313|Proteomes:UP000254426};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:RID96179.1, ECO:0000313|Proteomes:UP000266448}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCOM 1039 {ECO:0000313|EMBL:RID96179.1,
RC   ECO:0000313|Proteomes:UP000266448};
RA   Kook J.-K., Park S.-N., Lim Y.K.;
RT   "Genome sequencing of Streptococcus constellatus KCOM 1039.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:QRP82520.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FDAARGOS_1208 {ECO:0000313|EMBL:QRP82520.1};
RA   Sproer C., Gronow S., Severitt S., Schroder I., Tallon L., Sadzewicz L.,
RA   Zhao X., Boylan J., Ott S., Bowen H., Vavikolanu K., Mehta A.,
RA   Aluvathingal J., Nadendla S., Lowell S., Myers T., Yan Y., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx tests.";
RL   Submitted (FEB-2021) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000256|ARBA:ARBA00007249, ECO:0000256|HAMAP-
CC       Rule:MF_00118}.
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DR   EMBL; JWIY01000001; KIC78886.1; -; Genomic_DNA.
DR   EMBL; LQXU01000007; KXU02771.1; -; Genomic_DNA.
DR   EMBL; CP069558; QRP82520.1; -; Genomic_DNA.
DR   EMBL; QWKV01000001; RID96179.1; -; Genomic_DNA.
DR   EMBL; UHFC01000002; SUN40845.1; -; Genomic_DNA.
DR   RefSeq; WP_003023932.1; NZ_UHFC01000002.1.
DR   AlphaFoldDB; A0A0C1K7P6; -.
DR   STRING; 862969.SCI_1347; -.
DR   GeneID; 58100039; -.
DR   PATRIC; fig|76860.7.peg.229; -.
DR   eggNOG; COG0050; Bacteria.
DR   OrthoDB; 9804504at2; -.
DR   Proteomes; UP000031339; Unassembled WGS sequence.
DR   Proteomes; UP000073019; Unassembled WGS sequence.
DR   Proteomes; UP000254426; Unassembled WGS sequence.
DR   Proteomes; UP000266448; Unassembled WGS sequence.
DR   Proteomes; UP000647144; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01884; EF_Tu; 1.
DR   CDD; cd03697; EFTU_II; 1.
DR   CDD; cd03707; EFTU_III; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
DR   InterPro; IPR041709; EF-Tu_GTP-bd.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR033720; EFTU_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   NCBIfam; TIGR00485; EF-Tu; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00118}; Hydrolase {ECO:0000313|EMBL:KIC78886.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00118}.
FT   DOMAIN          10..207
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT   BINDING         84..88
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT   BINDING         139..142
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   398 AA;  44063 MW;  CB4843FE231D0CD9 CRC64;
     MAKEKYDRSK PHVNIGTIGH VDHGKTTLTA AITTVLARRL PSSVNQPKDY SSIDAAPEER
     ERGITINTAH VEYETAKRHY AHIDAPGHAD YVKNMITGAA QMDGAILVVA STDGPMPQTR
     EHILLSRQVG VKYLIVFMNK VDLVDDEELL ELVEMEIRDL LSEYDFPGDE IPVIQGSALK
     ALEGDEKYED IIMELMDTVD EYIPEPERDT DKPLLLPVED VFSITGRGTV ASGRIDRGTV
     KVNDEVEIVG IRDEIQKAVV TGVEMFRKQL DEGLAGDNVG VLLRGIQRDE IERGQVLAKP
     GSIHPHTKFK GEVYILTKEE GGRHTPFFNN YRPQFYFRTT DVTGSIELPA GTEMVMPGDN
     VTIDVELIHP IAVEQGTTFS IREGGRTVGS GMVTEIEA
//
ID   U2ZUC7_STRAP            Unreviewed;       398 AA.
AC   U2ZUC7;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Elongation factor Tu {ECO:0000256|ARBA:ARBA00029554, ECO:0000256|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118};
GN   ORFNames=ANG6_0633 {ECO:0000313|EMBL:GAD46138.1};
OS   Streptococcus anginosus T5.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus; Streptococcus anginosus group.
OX   NCBI_TaxID=1163302 {ECO:0000313|EMBL:GAD46138.1, ECO:0000313|Proteomes:UP000016981};
RN   [1] {ECO:0000313|EMBL:GAD46138.1, ECO:0000313|Proteomes:UP000016981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T5 {ECO:0000313|EMBL:GAD46138.1,
RC   ECO:0000313|Proteomes:UP000016981};
RA   Maruyama F., Sakurai A., Ogura Y., Homma H., Takahashi N., Ohtsubo Y.,
RA   Hoshino T., Okahashi N., Nakagawa I., Kimura S., Fujiwara T., Hayashi T.,
RA   Shintani S.;
RT   "Genome Sequences of seven clinical isolates and type strains of anginosus
RT   group streptococci.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000256|ARBA:ARBA00007249, ECO:0000256|HAMAP-
CC       Rule:MF_00118}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAD46138.1}.
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DR   EMBL; BASY01000004; GAD46138.1; -; Genomic_DNA.
DR   RefSeq; WP_003023932.1; NZ_BASY01000004.1.
DR   AlphaFoldDB; U2ZUC7; -.
DR   GeneID; 58100039; -.
DR   Proteomes; UP000016981; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01884; EF_Tu; 1.
DR   CDD; cd03697; EFTU_II; 1.
DR   CDD; cd03707; EFTU_III; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
DR   InterPro; IPR041709; EF-Tu_GTP-bd.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR033720; EFTU_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   NCBIfam; TIGR00485; EF-Tu; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00118}.
FT   DOMAIN          10..207
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT   BINDING         84..88
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT   BINDING         139..142
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   398 AA;  44063 MW;  CB4843FE231D0CD9 CRC64;
     MAKEKYDRSK PHVNIGTIGH VDHGKTTLTA AITTVLARRL PSSVNQPKDY SSIDAAPEER
     ERGITINTAH VEYETAKRHY AHIDAPGHAD YVKNMITGAA QMDGAILVVA STDGPMPQTR
     EHILLSRQVG VKYLIVFMNK VDLVDDEELL ELVEMEIRDL LSEYDFPGDE IPVIQGSALK
     ALEGDEKYED IIMELMDTVD EYIPEPERDT DKPLLLPVED VFSITGRGTV ASGRIDRGTV
     KVNDEVEIVG IRDEIQKAVV TGVEMFRKQL DEGLAGDNVG VLLRGIQRDE IERGQVLAKP
     GSIHPHTKFK GEVYILTKEE GGRHTPFFNN YRPQFYFRTT DVTGSIELPA GTEMVMPGDN
     VTIDVELIHP IAVEQGTTFS IREGGRTVGS GMVTEIEA
//
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