ID   IF2_CLOPS               Reviewed;         679 AA.
AC   Q0SSD4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CPR_1658;
OS   Clostridium perfringens (strain SM101 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=289380;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM101 / 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; CP000312; ABG87394.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0SSD4; -.
DR   SMR; Q0SSD4; -.
DR   EnsemblBacteria; ABG87394; ABG87394; CPR_1658.
DR   KEGG; cpr:CPR_1658; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000001824; 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_1000008234"
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;  74134 MW;  D3BDC18D6D4C4C87 CRC64;
     MSKIRVYELA KELRVPSKVL INVLMDEFGV EVKNHMSVIE DEDAALIKEL LAGSEANSEL
     VAEYEAELAE EVNNAAKKKK KRKKGSEDDS 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