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Database: UniProt
Entry: U2KKD5_9STRE
LinkDB: U2KKD5_9STRE
Original site: U2KKD5_9STRE 
ID   U2KKD5_9STRE            Unreviewed;       905 AA.
AC   U2KKD5;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000256|HAMAP-Rule:MF_00100};
GN   ORFNames=HMPREF1557_00676 {ECO:0000313|EMBL:ERJ77664.1};
OS   Streptococcus sobrinus W1703.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1227275 {ECO:0000313|EMBL:ERJ77664.1, ECO:0000313|Proteomes:UP000016617};
RN   [1] {ECO:0000313|EMBL:ERJ77664.1, ECO:0000313|Proteomes:UP000016617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W1703 {ECO:0000313|EMBL:ERJ77664.1,
RC   ECO:0000313|Proteomes:UP000016617};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA   Wilson R.K.;
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: One of the essential components for the initiation of protein
CC       synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC       and promotes its binding to the 30S ribosomal subunits. Also involved
CC       in the hydrolysis of GTP during the formation of the 70S ribosomal
CC       complex. {ECO:0000256|ARBA:ARBA00025162, ECO:0000256|HAMAP-
CC       Rule:MF_00100, ECO:0000256|RuleBase:RU000644}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00007733, ECO:0000256|HAMAP-Rule:MF_00100,
CC       ECO:0000256|RuleBase:RU000644}.
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:ERJ77664.1}.
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DR   EMBL; AWVA01000036; ERJ77664.1; -; Genomic_DNA.
DR   RefSeq; WP_019780517.1; NZ_KI259707.1.
DR   AlphaFoldDB; U2KKD5; -.
DR   GeneID; 57973377; -.
DR   PATRIC; fig|1227275.3.peg.600; -.
DR   HOGENOM; CLU_006301_5_1_9; -.
DR   OrthoDB; 9811804at2; -.
DR   Proteomes; UP000016617; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01887; IF2_eIF5B; 1.
DR   CDD; cd03702; IF2_mtIF2_II; 1.
DR   CDD; cd03692; mtIF2_IVc; 1.
DR   Gene3D; 1.10.10.2480; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR   HAMAP; MF_00100_B; IF_2_B; 1.
DR   InterPro; IPR044145; IF2_II.
DR   InterPro; IPR006847; IF2_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR000178; TF_IF2_bacterial-like.
DR   InterPro; IPR015760; TIF_IF2.
DR   InterPro; IPR023115; TIF_IF2_dom3.
DR   InterPro; IPR036925; TIF_IF2_dom3_sf.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   NCBIfam; TIGR00487; IF-2; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43381:SF5; TRANSLATION INITIATION FACTOR IF-2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   Pfam; PF04760; IF2_N; 2.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 2.
DR   PROSITE; PS51722; G_TR_2; 1.
DR   PROSITE; PS01176; IF2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00100};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW   Rule:MF_00100};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00100};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00100}.
FT   DOMAIN          407..576
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          28..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..558
FT                   /note="G-domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   COMPBIAS        42..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..154
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..222
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..275
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..290
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         416..423
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         462..466
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         516..519
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   905 AA;  99520 MW;  F157CD6DD58F1C1E CRC64;
     MSKKRLYEIA KELGKPSKDV VEKAKSLGLD VKSHASSVEE ADAKRISSSF SATKASAPKA
     SQSESKPAPK PTSTPKSEVE AKPAQEVKAA SEKSVQPKPA AKPKPKIRNF KAEREAKAKA
     AAERHQNQGK GKQNNRGDRR NNDRRRDNRS GNRNDQRNNR NQANQGPRID FKARATALKA
     EQNAEYSRQS EDRFRQEQES KSVAARRQEE ARQNKRKAQE EAQAQPSKPT PAAAPTVAAK
     PAPAKAKDTR RKKANRSDKS RDFSHQNEDG PKQSKNKKWN NQNQVRNQRN SNWNHKKKKG
     KNNRKDQAPK PVTERKFHEL PKEFEYTEGM TVADIAKRIK REPAEIVKKL FMMGVMATQN
     QSLDGDTIEL LMVDYGIDPK KKVEVDDADI ERFFVDDDYL NEDQLVERAP VVTIMGHVDH
     GKTTLLDTLR NSRVATGEAG GITQHIGAYQ INANGKKITF LDTPGHAAFT SMRARGASVT
     DVTILIVAAD DGVMPQTVEA INHSKAAGVP IIVAINKIDK PGANPERVIG ELAEHGVIST
     AWGGESEFVE ISAKFGQNID ELLETVLLVA EMEELKADPT VRAIGTVIEA RLDKGKGAVA
     TLLVQQGTLH VQDPIVAGNT FGRVRAMTND LGRRVKEAAP STPVSITGLN EAPMAGDHFA
     IYEDEKAARA AGEERAKRAL LKQRQITHRV SLENLFDTLK DGEVKSVNVI IKADVQGSVE
     ALATSLQKIE VEGAKVTIVH SAVGAINESD ITLAEASNAV VIGFNVRPTP QARAQAETDE
     VEIRLHSIIY KVIEEIEDAM KGMLDPEFEE KIIGEALIRE TFKVSKVGTI GGFLVTSGKV
     TRDSSVRVIR DGVVIYDGKL ASLRHFKDDV KEIGNAQEGG LMIEGYNDIK VDDTVEAYVM
     EEIKR
//
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