IF2_CLOB1
ID IF2_CLOB1 Reviewed; 688 AA.
AC A7FVZ3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CLB_2282;
OS Clostridium botulinum (strain ATCC 19397 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441770;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19397 / 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000726; ABS34758.1; -; Genomic_DNA.
DR RefSeq; WP_003388357.1; NC_009697.1.
DR AlphaFoldDB; A7FVZ3; -.
DR SMR; A7FVZ3; -.
DR GeneID; 5186673; -.
DR KEGG; cba:CLB_2282; -.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
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_1000008229"
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
