IF2_CLOD6
ID IF2_CLOD6 Reviewed; 646 AA.
AC Q18BH4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CD630_13090;
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630;
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
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; AM180355; CAJ68167.1; -; Genomic_DNA.
DR RefSeq; WP_003438306.1; NZ_CP010905.2.
DR RefSeq; YP_001087805.1; NC_009089.1.
DR AlphaFoldDB; Q18BH4; -.
DR SMR; Q18BH4; -.
DR STRING; 272563.CD630_13090; -.
DR PRIDE; Q18BH4; -.
DR EnsemblBacteria; CAJ68167; CAJ68167; CD630_13090.
DR GeneID; 66353712; -.
DR KEGG; cdf:CD630_13090; -.
DR KEGG; pdc:CDIF630_01465; -.
DR PATRIC; fig|272563.120.peg.1369; -.
DR eggNOG; COG0532; Bacteria.
DR OMA; NRDNRTG; -.
DR PhylomeDB; Q18BH4; -.
DR BioCyc; PDIF272563:G12WB-1445-MON; -.
DR Proteomes; UP000001978; 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; Reference proteome.
FT CHAIN 1..646
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008232"
FT DOMAIN 146..315
FT /note="tr-type G"
FT REGION 155..162
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 180..184
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 201..204
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 255..258
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 291..293
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 155..162
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 201..205
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 255..258
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 646 AA; 69711 MW; 7F74BD9FD52327D9 CRC64;
MSKTRVYQIA EELNISNEEL INKLAELDIN VTDKDSVLEG EELELALEML GEDLSQENGN
VIEIDGKLTV QVLATKLDKS PSEIIMKLMK MGTMATINQE ISFEIAALAA KDYGFELTVA
ESDDTEALEI EALMEIEEDK EEDLKPRPPV VTVMGHVDHG KTSLLDAIRK TDVISGEAGG
ITQHIGASEV KINGHKIVFL DTPGHEAFTS MRARGAQVTD IAILVVAADD GIMPQTVEAI
NHAKAAGVPL IVAINKIDKP GANPDKVKQE LADQGLLVED WGGEVIAVPV SAKKKEGIDT
LLEMVLLVAE MEELRANPNK RAVGTVIEAE LDKGRGPVAT VLVQGGTLTV GDPIVAGVAC
GKVRAMINAK GKRVKTAGPS TAVEILGLSE VPQGGDQFVE VPTDKIARSV AARRQQIVRD
EMLKSTQRLS LDALFSQMSE GSIKDLNIVI KADVQGSVQA VKQSLEKLSN EEVQVKVIHG
GVGAVTESDI LLAAASNAII IGFNVRPVPG AESLGEKENV DIRTYTIIYK AIEDIQAAMT
GMLDPEYVDE ETGKAEIREI YKISGVGTVA GCYVTNGKIF RNCKVRLVRD SIIIHEGELA
ALKRFKDDVK EVNSGYECGM SFVNYNDIKE GDIVEAYITK EVERKL
