IF2_CLOAB
ID IF2_CLOAB Reviewed; 693 AA.
AC Q97I51;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CA_C1802;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK79767.1; -; Genomic_DNA.
DR PIR; D97122; D97122.
DR RefSeq; NP_348427.1; NC_003030.1.
DR RefSeq; WP_010965108.1; NC_003030.1.
DR AlphaFoldDB; Q97I51; -.
DR SMR; Q97I51; -.
DR STRING; 272562.CA_C1802; -.
DR EnsemblBacteria; AAK79767; AAK79767; CA_C1802.
DR GeneID; 44998296; -.
DR KEGG; cac:CA_C1802; -.
DR PATRIC; fig|272562.8.peg.2008; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000814; 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..693
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137193"
FT DOMAIN 193..362
FT /note="tr-type G"
FT REGION 78..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..209
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 227..231
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 248..251
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 302..305
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 338..340
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 202..209
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 248..252
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 302..305
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 693 AA; 76337 MW; CA0D2050F13E4082 CRC64;
MPKVRIYELS KELGRSSKEL INILHDEFGI VVKNHMSVID EEDAELIKEM LSESNDEDKK
SDLVEEYEDM ISDSIKVRKN KKVKQKDKDK ENTDEDEEEE QEFDDVIEIE NTITVKDLAD
KLKKPITEVI KELMFMGVMA AINQEIDFET SSKVAAKFKV DVIQKAEEAD KKELKSEFEN
EFEEDEDEGT WIKRPPVVTV MGHVDHGKTS LLDAIRKSSV TETEAGGITQ HIGAYTVKMN
EGKVTFLDTP GHEAFTAMRA RGAEITDVVI LVVAADDGIM PQTKEAINHC KAANVPIVVA
INKIDKPGAN IDRVKQELTE HGLIPEDWGG DTICVPVSAK TKQGLDSLIE MTILTADVMD
LKADPKRHAR GTVIEGKLDK GRGPVASLIV QNGTLKVGNS IIVGSTYGRI RAMFDDKGKK
IKSAGPSVPV EILGLSDVPE AGDKFNVVKD EKTARNMAKI RVEKLRSANL ASKHKVSLED
LYSQIQEGKV KELGIIVKAD VQGSVEAVKQ SFEKLSTDAV KVRVIHGAVG AITETDVILA
SASNAIIIGF NVRPDNNASA LAEKEKVDIK TYRVIYTAID DIKSAMIGML DPEYKEEVIG
NAEVRHIYKI SSIGTVAGCY VTSGKITRSS SIRVIRDGIV ILEGELASLK RFKDDAKEVA
RGFECGLTID KFNDIKEGDV IEAFQMVKVK QEG
