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IF2_CLOP1
ID   IF2_CLOP1               Reviewed;         679 AA.
AC   Q0TPR7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CPF_1940;
OS   Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS   6125 / NCTC 8237 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC   Type A;
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA   Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA   Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA   Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA   Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA   Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT   Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(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; CP000246; ABG83328.1; -; Genomic_DNA.
DR   RefSeq; WP_003449445.1; NC_008261.1.
DR   AlphaFoldDB; Q0TPR7; -.
DR   SMR; Q0TPR7; -.
DR   STRING; 195103.CPF_1940; -.
DR   PRIDE; Q0TPR7; -.
DR   EnsemblBacteria; ABG83328; ABG83328; CPF_1940.
DR   GeneID; 29570959; -.
DR   KEGG; cpf:CPF_1940; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_9; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000001823; 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..679
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008233"
FT   DOMAIN          178..347
FT                   /note="tr-type G"
FT   REGION          187..194
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          212..216
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          233..236
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          287..290
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          323..325
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         187..194
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         233..237
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         287..290
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   679 AA;  74161 MW;  AB4CF8439D78DF06 CRC64;
     MSKIRVYELA KELRVPSKVL INVLMDEFGV EVKNHMSVIE DEDAALIKEL LAGSEANSEL
     VAEYEAELAE EVNNAAKKKK KRKKGSEDDN LEQDVEVIEI GKTITVKELA EKLNKPVNDV
     IKTLIFTGVM AAINQEIDFE TAEKVAEKYE VAVYEKEEEN TLEEFEEETD VEEENLAKRP
     PIITVMGHVD HGKTSLLDAI RKSKVTSTEA GGITQHIGAY TVEVNGETLT FLDTPGHEAF
     TAMRARGAQI TDVVILVVAA DDGIMPQTVE AINHCKAANV PMIVAINKMD REGANPDRVK
     QELTEHGLVV EDWGGDIIAV PVSAKTRENI DTLLEMVLLT SEMQELKADA GRKAKGTVVE
     AKLDKGRGAV ATLLVQNGTL HMGDSIIVGS TYGRIRAMFD DSGKKIKSAG PSIPVEVLGL
     SEVPAAGDRF TVVKDEKTAR NMAEARKEKI RQESFATSHR VSLEDLYSQI KEGSVKELSV
     IVKADVQGSV EAIKASLEKL STDDVKVRVI HGAVGAISET DITLAAASNA IVIGFNVRPD
     NNAVAASERD GVEVKTYRVI YDAIEDIKSA MIGMLDPEYK EVVLGTAEIR ATYKISNVGT
     IAGGYVLTGK LVRNADVRVI REGIVIFESK LASLKRFKDD VKEVNAGYEC GFSVEKFNDI
     KEGDIIEAYT MEAVQRKEL
 
 
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