IF2_MYCCT
ID IF2_MYCCT Reviewed; 620 AA.
AC Q2SSE6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=MCAP_0333;
OS Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS / NCTC 10154).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=340047;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000123; ABC01401.1; -; Genomic_DNA.
DR RefSeq; WP_011387218.1; NC_007633.1.
DR AlphaFoldDB; Q2SSE6; -.
DR SMR; Q2SSE6; -.
DR EnsemblBacteria; ABC01401; ABC01401; MCAP_0333.
DR GeneID; 23778711; -.
DR KEGG; mcp:MCAP_0333; -.
DR HOGENOM; CLU_006301_5_1_14; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR PhylomeDB; Q2SSE6; -.
DR Proteomes; UP000001928; 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; 1.
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.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..620
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008280"
FT DOMAIN 119..288
FT /note="tr-type G"
FT REGION 128..135
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 153..157
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 175..178
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 229..232
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 265..267
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 128..135
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 175..179
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 229..232
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 620 AA; 68659 MW; 9DEB5CBD7EE9275C CRC64;
MKKPVKNIKK QKAQNQTKNI KKQLKEEVNT GLIDGIFVYT EPLSILEFAT KINKPVTVIL
KHYFNQGLLL NQNTLLTEEQ MGELCLEFGF DFKKETSVTK ENILETLLDT VDDEKHLKER
PPIVTIMGHV DHGKTTLLDS IKNSNVVASE AGGITQAIGA YQITTKNNKK ITFIDTPGHE
AFTEMRSRGA NVTDIVVLIV AADDGVMPQT EEAIDHAKLA NVPIIVFINK IDKPGSDPNR
VKTELMKYGL VAEEFGGDIP FIEGSAIKKI NLDKLEDTII LISELENLKA NPDRFASGVV
LEAHLDKAKG PVASVLVQQG SLEIKDIMVV GTTFGSIKHI EDEFKHKVLK AEPSKPVVVY
GLNQVPKAGD KFVVINDEKM AREISEAQLK KQQEEERRTK QAFTLDAIKQ HIDEGELKNI
TLIIKADTQG SVEALKNSLS KINISGVKIN IIRASVGAIS LSDISLASTV RDGLVIVYGF
NVRPDAIVRK KAEEDRIEIR LHNIIYKLIE ELEDAAKGIL DPEIKEVVLG QAQVRALFRH
SAIGTIGGFY VVDGAITRNA KIRVIRNGVV VYDGEINSLQ HQKQDAKEVK AGFEGALTIK
NFNDIKEGDI FEAYKLEQVK