IF2_VIBPA
ID IF2_VIBPA Reviewed; 905 AA.
AC Q87M02;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=VP2456;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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; BA000031; BAC60719.1; -; Genomic_DNA.
DR RefSeq; NP_798835.1; NC_004603.1.
DR RefSeq; WP_005481598.1; NC_004603.1.
DR AlphaFoldDB; Q87M02; -.
DR SMR; Q87M02; -.
DR STRING; 223926.28807454; -.
DR PRIDE; Q87M02; -.
DR EnsemblBacteria; BAC60719; BAC60719; BAC60719.
DR GeneID; 1189969; -.
DR KEGG; vpa:VP2456; -.
DR PATRIC; fig|223926.6.peg.2357; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000002493; Chromosome 1.
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; 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..905
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137280"
FT DOMAIN 404..573
FT /note="tr-type G"
FT REGION 30..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..420
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 438..442
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 459..462
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 513..516
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 549..551
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 33..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 413..420
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 459..463
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 513..516
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 905 AA; 99396 MW; CA2A20F619B0A717 CRC64;
MTQLTVKALS DEIGTPVDRL IEQLADAGMK KASSDNVTDE EKQKLLSHLK KEHGDKSGDA
EPTRLTLQRK TRSTLSVNAG GGKSKNVQVE VRKKRTYVKR STIEDEAKRE AEEVAKREAE
EAAKRVAEET AKREAEEAAK REAEDAVKRE AEEKAKREAE EKAKRDADTN AQRNAEEKAK
RDAEEKIKQE AARKEADELK RRQEEEAKRK AEEESQRKLE EARELAEKNK ERWSAAEEKK
GDMEDTDYHV TTSQYAREAE DEADRKEEAG RRNKKKKKPS TKDEQARNSG RSQRGGKGGR
KGKLAKPTSM QHGFDKSATV AKQDVVIGET IVLSELANKM SVKATEVIKV MMKMGAMATI
NQVIDQETAQ LVAEEMGHKV VLRKENELEE AVLSDRDTNA ESVPRAPVVT IMGHVDHGKT
STLDYIRRTH VASGEAGGIT QHIGAYHVET ENGMITFLDT PGHAAFTAMR ARGAQATDIV
VLVVAADDGV MPQTVEAIQH AKAAGVPLIV AVNKIDKEDA NPDNVKNELA QYDVIPEEWG
GENMFVHISA KQGTNIDGLL EAILLQSEVL ELTAVKEGMA SGVVVESRLD KGRGPVATVL
VQSGTLHKGD IVLCGQEYGR VRAMRDELGQ EITEAGPSIP VEILGLSGVP ASGDEATVVR
DERKAREVAN YRAGKFREVK LARQQKSKLE NMFSNMTAGE VAELNVVLKA DVQGSVEAIA
DSLLKLSTDE VKVNIVGSGV GGITETDVVL AEASNAIILG FNVRADASAR RAVEAAAVDL
RYYSIIYQLI DEVKQAMGGM LAPEFKQEII GLAEVRDVFK SPKLGAIAGC MVTEGLIKRN
NPIRVLRDNV VIYEGELESL RRFKDDVQEV KNGYECGIGV KNYNDVRVGD QIEVFEIVEI
QRTLD
