IF2_VIBA3
ID IF2_VIBA3 Reviewed; 896 AA.
AC B7VJH7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=VS_2482;
OS Vibrio atlanticus (strain LGP32) (Vibrio splendidus (strain Mel32)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=575788;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LGP32;
RA Mazel D., Le Roux F.;
RT "Vibrio splendidus str. LGP32 complete genome.";
RL Submitted (FEB-2009) 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: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; FM954972; CAV19641.1; -; Genomic_DNA.
DR RefSeq; WP_009847541.1; NC_011753.2.
DR AlphaFoldDB; B7VJH7; -.
DR SMR; B7VJH7; -.
DR STRING; 575788.VS_2482; -.
DR EnsemblBacteria; CAV19641; CAV19641; VS_2482.
DR KEGG; vsp:VS_2482; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000009100; 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..896
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000190643"
FT DOMAIN 395..564
FT /note="tr-type G"
FT REGION 49..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..411
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 429..433
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 450..453
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 504..507
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 540..542
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 60..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 404..411
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 450..454
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 504..507
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 896 AA; 97525 MW; 1E52CC5690893C9E CRC64;
MTQLTVKALS EEIGTPVDRL IEQLADAGMK KAGSDQVTDS EKQTLLTHLK KEHGDTSGET
EPTRLTLQRK TRSTLSVAAG GGKSKDVQVE VRKKRTYVKR STIEDEAKRE AEEVANREAE
EKAQRDAEEQ AKRDAAEKAQ REAEAKVTRE ADAKREAEEK AQRAQAEKAK KDMNSKNADA
NAQAKKEADE LKARQEQEAT RKAEAEAAKL VEEARKLAEE NQERWSEEEK KKKEQEKSAD
YHVTTSTYAR EAEDAADKKD EKAPRRRKKK PAPATQPGNN RGGRNQRGRG GKGKLAKPTS
MQQGFDKSAT VAKSDVAIGE TIVVSELASK MSVKATEVIK VMMKMGAMAT INQVIDQETA
QLVAEEMGHK VILRKENELE EAVLADRDSD AIAEGRAPVV TIMGHVDHGK TSTLDYIRKA
HVASGEAGGI TQHIGAYHVD TDNGMITFLD TPGHAAFTAM RARGAQATDI VVLVVAADDG
VMPQTIEAIQ HAKAAGVPLI VAVNKIDKEG ANPDNVKNEL AQYDVIPEEW GGENIFVHIS
AKQGTNIDGL LESILLQSEV LELTAVKEGM ASGVVVESRL DKGRGPVATV LVQSGTLNKG
DIVLCGQEYG RVRAMRDENG KDIETAGPSI PVEILGLSGV PASGDEATVV RDERKAREVA
NYRQGKFRDV KLARQQKAKL ENMFANMTAG EVAELNVVLK ADVQGSVEAI ADSLLKLSTD
EVKVNIVGSG VGGITETDAT LAAASNAIIL GFNVRADATA RNTVQNENLD LRYYSIIYQL
IDEVKQAMGG MLAPEFRQEI IGLAQVRDVF KSPKLGAIAG CIVTEGTIKR SNPIRVLREN
VVIYEGELES LRRFKDDVQE VKNGYECGVG VKNYNDVRVG DQIEVFEIVE VKRTLD
