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IF2_CLOBH
ID   IF2_CLOBH               Reviewed;         688 AA.
AC   A5I4J3; A7G5P4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN   OrderedLocusNames=CBO2418, CLC_2265;
OS   Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX   PubMed=17519437; DOI=10.1101/gr.6282807;
RA   Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA   Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA   Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA   Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA   Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA   Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA   White B., Whithead S., Parkhill J.;
RT   "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT   Hall A and comparative analysis of the clostridial genomes.";
RL   Genome Res. 17:1082-1092(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
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; CP000727; ABS37445.1; -; Genomic_DNA.
DR   EMBL; AM412317; CAL83965.1; -; Genomic_DNA.
DR   RefSeq; WP_003388357.1; NC_009698.1.
DR   RefSeq; YP_001254914.1; NC_009495.1.
DR   RefSeq; YP_001388109.1; NC_009698.1.
DR   AlphaFoldDB; A5I4J3; -.
DR   SMR; A5I4J3; -.
DR   GeneID; 5186673; -.
DR   KEGG; cbh:CLC_2265; -.
DR   KEGG; cbo:CBO2418; -.
DR   PATRIC; fig|413999.7.peg.2395; -.
DR   HOGENOM; CLU_006301_5_1_9; -.
DR   OMA; NRDNRTG; -.
DR   PRO; PR:A5I4J3; -.
DR   Proteomes; UP000001986; Chromosome.
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; 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; PF04760; IF2_N; 2.
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..688
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008230"
FT   DOMAIN          187..354
FT                   /note="tr-type G"
FT   REGION          53..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          196..203
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          221..225
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          242..245
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          296..299
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          332..334
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        53..72
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         196..203
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         242..246
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         296..299
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   688 AA;  75810 MW;  D062EAD1B067114B CRC64;
     MAKIRVYELA KELNISSKEL ITLLEEEFSV EVKNHMSAIE DEDANLIKEL LSGKEKSEKT
     KEEDDEIETT AKNPIKESMN NKKSNKRDDK NEKVNTENAE DMGIITMTSD TITVKEISDK
     LEKSYAEVIK ELMLMGVMAS VNQEINFEMA EKLAAKFDME ILKEDEDEKE DLEDILKDNE
     EEEYLQKRSP IITVMGHVDH GKTSLLDAIR KSKVTSTEAG GITQHIGAYT VELNGEAITF
     LDTPGHAAFT AMRARGAQVT DIVILVVAAD DGIMPQTQEA ISHCKAANVP LIVAINKIDR
     PGANIDKVKQ ELTEYGLVAE DWGGDTICVP VSAHTKEGID DLLEMILLSS EILELKANPN
     RKAKGTVVEA KLDKGRGPVA TLLIQNGTLR VGDSIVVGST YGRIRAMFND KGRNIESAGP
     STPVEILGLS EVPEAGDKFY QVKEEKTARG IADKRKEKIR DEYLQSTHKV SLEDLYNQIQ
     EGTVKELGLI VKADVQGSVE ALKQSLEKLS TEEVKVRVIH GGVGAINETD VTLATASNGI
     ILGFNVRPDN NAIIASERDG VDIKTYRVIY DAIEDIKSAM LGMLEPEFKE VVIGTAEVRQ
     VYKISSVGTI AGAYIQTGKL ARNAGARVIR DGIVIFESEL ASLKRFKDDA KEVAQGYECG
     LSIEKFNDIK EGDIIECFIM EEIKKKTL
 
 
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