IF2_VIBVY
ID IF2_VIBVY Reviewed; 907 AA.
AC Q7MI09;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=VV2708;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(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; BA000037; BAC95472.1; -; Genomic_DNA.
DR RefSeq; WP_011151080.1; NC_005139.1.
DR AlphaFoldDB; Q7MI09; -.
DR SMR; Q7MI09; -.
DR STRING; 672.VV93_v1c24250; -.
DR PRIDE; Q7MI09; -.
DR EnsemblBacteria; BAC95472; BAC95472; BAC95472.
DR KEGG; vvy:VV2708; -.
DR PATRIC; fig|196600.6.peg.2704; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002675; Chromosome I.
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..907
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137282"
FT DOMAIN 406..575
FT /note="tr-type G"
FT REGION 26..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..422
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 440..444
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 461..464
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 515..518
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 551..553
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 33..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 415..422
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 461..465
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 515..518
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 907 AA; 99604 MW; 2641FB2D71228F2D CRC64;
MTQLTVKALS EEIGTPVDRL LEQLADAGMK KSSSDQVSDE EKQKLLTHLK KEHGDTSGDA
EPTRLTLQRK TRSTLSVNAG GGKSKDVQIE VRKKRTYVKR SAIEDEAKRE AEEAAQREAE
EAAKRAAEEA AKREAEEAAK REAEEKAKRE AEEAAKREAE KSVDRDAEEK AKRDAEGKAK
RDAEEKVKQE AARKEAEELK RRQEEEAKRK AEEESQRKLE EAREMAEKNK ERWSAAEENK
GDMEDTDYHV TTSQYAREAE DEADRKEEEA RRRKKKTKSS AKASENDERG GPRVQRGGKG
GRKGKLSKPK SMQHGFDKSA VVAKSDVVIG ETIVVSELAN KMSVKATEVI KIMMKMGAMA
TINQVIDQET AQLVAEEMGH KVVLRKENEL EEAVLSDRDN MFEAVPRAPV VTIMGHVDHG
KTSTLDYIRR THVASGEAGG ITQHIGAYHV ETENGMITFL DTPGHAAFTA MRARGAQATD
IVVLVVAADD GVMPQTVEAI QHAKAAGVPL IVAVNKIDKE EANPDNVKNE LSQYNVMPEE
WGGENMFVHI SAKQGTNIDQ LLETILLQAE VLELTAVKEG MASGVVVESR LDKGRGPVAT
VLVQSGTLRK GDIVLCGQEY GRVRAMRDEI GNEVNEAGPS IPVEILGLSG VPAAGDEATV
VRDERKAREV ANYRAGKFRE VKLARQQKSK LENMFSNMAA GDVAELNIVL KADVQGSVEA
IADSLTKLST EEVKVNIVGS GVGGITETDA VLAEASNAII LGFNVRADAS ARRAIEAASI
DLRYYSIIYQ LIDEVKQAMS GMLAPEFKQE IIGLAEVRDV FKSPKLGAIA GCMVTEGLIK
RNAPIRVLRD NVVIYEGELE SLRRFKDDVA EVKNGYECGI GVKNYNDVRV GDQIEVFETI
EIKRTID
