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Database: UniProt
Entry: A0A127VTS6_SPOPS
LinkDB: A0A127VTS6_SPOPS
Original site: A0A127VTS6_SPOPS 
ID   A0A127VTS6_SPOPS        Unreviewed;       395 AA.
AC   A0A127VTS6;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
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:AMQ04733.1};
GN   ORFNames=AZE41_01425 {ECO:0000313|EMBL:AMQ04733.1};
OS   Sporosarcina psychrophila (Bacillus psychrophilus).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX   NCBI_TaxID=1476 {ECO:0000313|EMBL:AMQ04733.1, ECO:0000313|Proteomes:UP000071057};
RN   [1] {ECO:0000313|EMBL:AMQ04733.1, ECO:0000313|Proteomes:UP000071057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6497 {ECO:0000313|EMBL:AMQ04733.1,
RC   ECO:0000313|Proteomes:UP000071057};
RA   Yan W.;
RT   "Complete genome sequence of the Sporosarcina psychrophila DSM6497, a
RT   psychrophila Bacillus that can mediate the Ca2+ precipitation.";
RL   Submitted (MAR-2016) 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; CP014616; AMQ04733.1; -; Genomic_DNA.
DR   RefSeq; WP_067204738.1; NZ_CP014616.1.
DR   AlphaFoldDB; A0A127VTS6; -.
DR   STRING; 1476.AZE41_01425; -.
DR   KEGG; spsy:AZE41_01425; -.
DR   OrthoDB; 9804504at2; -.
DR   Proteomes; UP000071057; 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};
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..204
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         81..85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT   BINDING         136..139
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   395 AA;  43031 MW;  AB19B04368DF74A1 CRC64;
     MGKEKFDRSK QHANVGTIGH VDHGKTTLTA AIATVLAKRL GGTAASYADV DNAPEEKERG
     ITINTSHVEY ETATRHYAHV DCPGHADYVK NMITGAAQMD GGILVVSAAD GPMPQTREHI
     LLSRQVGVPH LVVFMNKCDM VDDEELLELV EMEIRDLLSE YDFPGDDIPV IKGSALKALE
     GDEGYEDKIM ELMAAVDEYI PTPPRDTEKP FMMPVEDVFS ITGRGTVATG RVERGVVKIG
     DVVDIIGIVE EPKATTVTGV EMFRKLLDYA EAGDNIGALL RGVSRDDIQR GQVLAKPGTI
     VPHTKFTSEV YVLSKEEGGR HTPFFSNYRP QFYFRTTDVT GVIELPEGVE MVMPGDNIEM
     TIDLIAPIAL EEGTKFSIRE GGRTVGAGVV ATILK
//
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