ID IF2_CLOPE Reviewed; 679 AA.
AC Q8XJR8;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CPE1686;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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; BA000016; BAB81392.1; -; Genomic_DNA.
DR RefSeq; WP_003449445.1; NC_003366.1.
DR AlphaFoldDB; Q8XJR8; -.
DR SMR; Q8XJR8; -.
DR STRING; 195102.gene:10490950; -.
DR GeneID; 69449609; -.
DR KEGG; cpe:CPE1686; -.
DR HOGENOM; CLU_006301_5_1_9; -.
DR Proteomes; UP000000818; 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; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 1.10.10.2480; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR004161; EFTu-like_2.
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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
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..679
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137194"
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
//
