IF2_YERE8
ID IF2_YERE8 Reviewed; 892 AA.
AC A1JIW9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=YE0434;
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(2006).
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:0000255|HAMAP-Rule:MF_00100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00100}.
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DR EMBL; AM286415; CAL10560.1; -; Genomic_DNA.
DR RefSeq; WP_005175395.1; NC_008800.1.
DR RefSeq; YP_001004804.1; NC_008800.1.
DR AlphaFoldDB; A1JIW9; -.
DR SMR; A1JIW9; -.
DR STRING; 393305.YE0434; -.
DR PRIDE; A1JIW9; -.
DR EnsemblBacteria; CAL10560; CAL10560; YE0434.
DR GeneID; 67419362; -.
DR KEGG; yen:YE0434; -.
DR PATRIC; fig|393305.7.peg.530; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000000642; Chromosome.
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; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR013575; IF2_assoc_dom_bac.
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 PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF46955; SSF46955; 1.
DR SUPFAM; SSF50447; SSF50447; 2.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00487; IF-2; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..892
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008372"
FT DOMAIN 391..560
FT /note="tr-type G"
FT REGION 51..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..407
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 425..429
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 446..449
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 500..503
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 536..538
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 56..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 400..407
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 446..450
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 500..503
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 892 AA; 97336 MW; EFE033E1CA30AC20 CRC64;
MTDVTVKSLA DEIQTPVDRL VQQFADAGIK KSEVDSVTQQ EKETLLAHLN REHGSAPNKL
TLQRKTRSTL NIPSTGGKSK SVQIEVRKKR TYVNTPEAEQ AKAEEQAQRE AEEQAQREAE
AAAQKIAEEK AKRAAEEQAK REAAEKAKRQ AAEKEKVTNQ QTDEKTKPAQ TDKARREAEA
AELKRSVEEE TRRKVEEDAK RVAEEARKMA AENEGKWPEP VAEQTESADY HVTTSQHARA
AEDENDAKVE GDRRSRTRGG KATKQKKGNK LSESKADREE ARAVGRKGKR KPSTLQQSFN
KPVVAVNRDV VIGETVTVAE LANKMAVKGS QVIKAMMKLG AMATINQVID QETAQLVAEE
MGHKVILRRE NELEEALMSD RDTGAEAAAE HRAPVVTIMG HVDHGKTSLL DYIRSTKVAS
GEAGGITQHI GAYHVETENG MITFLDTPGH AAFTSMRARG AQATDIVVLV VAADDGVMPQ
TIEAIQHAKA ANVPVVVAVN KIDKPAADPN RVKTELIQHG IISEDFGGDV PFIEVSAKVG
TGIDDLLQAI LLQAEVMELK AVRTGMASGV VIESFLDKGR GPVATVLVQQ GTLNKGDIVL
CGFEYGRVRA MRDELGRDIT SAGPSIPVEI LGLSSVPAAG DEVTVVRDEK KAREVALYRQ
GKFREVKLAR QQKSKLENMF ANMTEGEVSE LNIVIKSDVQ GSCEAICDSL EKLSTDEVKV
RIVGSGVGGI TETDATLAAA SGAIILGFNV RADASARRVV ETEGLDLRYY SVIYSLIDEV
KQAMSGMLAP EYKQQIIGLA EVRDVFKSPK FGAIAGCMVT EGVIKRNNPI RVLRDNVVIY
EGELESLRRF KDDVNEVRNG MECGIGVKNY NDVRTGDVIE VFEIIEIKRT IA
