IF2_CLOBK
ID IF2_CLOBK Reviewed; 688 AA.
AC B1II49;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CLD_2222;
OS Clostridium botulinum (strain Okra / Type B1).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=498213;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okra / Type B1;
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; CP000939; ACA45084.1; -; Genomic_DNA.
DR RefSeq; WP_015957782.1; NC_010516.1.
DR AlphaFoldDB; B1II49; -.
DR SMR; B1II49; -.
DR EnsemblBacteria; ACA45084; ACA45084; CLD_2222.
DR KEGG; cbb:CLD_2222; -.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000008541; Chromosome.
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; 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.
FT CHAIN 1..688
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093775"
FT DOMAIN 187..354
FT /note="tr-type G"
FT REGION 54..95
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 54..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..95
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; 75742 MW; C9196EBAEC1C3BFA CRC64;
MAKIRVYELA KELNISSKEL ITLLEEEFSV EVKNHMSAIE DEDANLIKEL LSGKEKSEKT
KEEDDEIETT AKNPIKESTN NKKPNKRDDK NEKVNTENAE DMAIITITSE TITVKEISDK
LEKSYAEVIK ELMLMGVMAS VNQEINFEMA EKLAAKFDTE ILREDEDEED DLEDILRDNE
EEEYLQKRSP IITVMGHVDH GKTSLLDAIR KSKVTSTEAG GITQHIGAYT VELNGEAITF
LDTPGHAAFT AMRARGAQVT DIVILVVAAD DGIMPQTQEA ISHCKAANVP LIVAINKIDR
PGANIDKVKQ ELTEYGLVAE DWGGDTICVP VSAHTKEGID DLLEMILLSS EILELKANPN
RKAKGTVVEA KLDKGRGPVA TLLIQNGTLR VGDSIVVGST YGRIRAMFND KGRNIKSAGP
STPVEILGLS EVPEAGDKFY QVKEEKTARS IADKRKEKIR DEYLQSTHKV SLEDLYNQIQ
EGTVKELGLI VKADVQGSVE ALKQSLEKLS TGEVKVRVIH GGVGAINETD VTLATASNGI
ILGFNVRPDN NAIIASEKDG VDIKTYRVIY DAIEDIKSAM LGMLEPEFKE VVIGTAEVRQ
VYKISSVGTI AGAYIQTGKL ARNAGARVIR DGIVIFESEL ASLKRFKDDA KEVAQGYECG
LSIEKFNDIK EGDIIECFIM EEIKKKTL
