IF2_VIBCH
ID IF2_VIBCH Reviewed; 898 AA.
AC Q9KU80;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=VC_0643;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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; AE003852; AAF93809.1; -; Genomic_DNA.
DR PIR; A82298; A82298.
DR RefSeq; NP_230292.1; NC_002505.1.
DR RefSeq; WP_000192207.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KU80; -.
DR SMR; Q9KU80; -.
DR STRING; 243277.VC_0643; -.
DR DNASU; 2615433; -.
DR EnsemblBacteria; AAF93809; AAF93809; VC_0643.
DR GeneID; 57739360; -.
DR KEGG; vch:VC_0643; -.
DR PATRIC; fig|243277.26.peg.613; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR BioCyc; VCHO:VC0643-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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; 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; 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; Reference proteome.
FT CHAIN 1..898
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137279"
FT DOMAIN 397..566
FT /note="tr-type G"
FT REGION 51..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..413
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 431..435
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 452..455
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 506..509
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 542..544
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 60..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 406..413
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 452..456
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 506..509
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 898 AA; 98706 MW; F3369D5151414277 CRC64;
MTQITVKALS EEIGTPVDRL LEQLADAGMN KAVADHVSED EKQKLLAHLR KEHGDATGSE
PTRLTLQRKT RSTLSVNAGG GKSKNVQVEV RKKRTYVKRS SVEDEATREA EEAAMRAAEE
QAKREAEEAA QRAAEEKAKR EAEEAAKREA EAKRMAEEKA KRETQAATQP RSDEEKLKQE
AARKEAEALK RRQEEEARRK AEEESRRQLE KVRELAEKNG ERWSADKETV GDMQENTDYH
VTTSRYAREA EDEADLHEEG ARRRSTKANK RKMSSRDDNQ ERDSRPRGGK AGRKGRINKP
MSMQHGFDKT AVVAKADVVV GETIVVSELA QKMSVKATEV IKVMMKMGAM ATINQVIDQE
TAQLVAEEMG HKVVLRKENE LEEAILSDRD DKFEEVSRAP VVTIMGHVDH GKTSTLDYIR
RTHVASGEAG GITQHIGAYH VETPNGMITF LDTPGHAAFT AMRARGAQAT DIVVLVVAAD
DGVMPQTVEA IQHAKAAGVP LIVAVNKIDK DTANPDNVKT ELSQYNVMPE EWGGDNMFVH
ISAKQGTNID GLLEAILLQA EVLELKAVKQ GMASGVVIES RLDKGRGPVA TVLVQSGTLR
KGDIVLCGQE YGRVRAMRDE VGNEVEEAGP SIPVEILGLS GVPAAGDEAT VVRDERKARE
VANYRAGKFR EVKLARQQKS KLENMFSNMT AGDVAELNIV LKADVQGSVE AIADSLTKLS
TDEVKVNIVG SGVGGITETD AVLAAASNAI VVGFNVRADA SARRMIEAEN IDLRYYSIIY
QLIDEVKQAM SGMLSPEFKQ EIIGLAEVRD VFKSPKLGAI AGCMVTEGVI KRNAPIRVLR
DNVVIYEGEL ESLRRFKDDV AEVKNGYECG IGVKNYNDVR VGDQIEVFET IEIQRTID
