IF2_BACMK
ID IF2_BACMK Reviewed; 688 AA.
AC A9VT50;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN OrderedLocusNames=BcerKBAB4_3635;
OS Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315730;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBAB4;
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
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; CP000903; ABY44806.1; -; Genomic_DNA.
DR RefSeq; WP_012261584.1; NC_010184.1.
DR AlphaFoldDB; A9VT50; -.
DR SMR; A9VT50; -.
DR STRING; 315730.BcerKBAB4_3635; -.
DR EnsemblBacteria; ABY44806; ABY44806; BcerKBAB4_3635.
DR KEGG; bwe:BcerKBAB4_3635; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000002154; 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..688
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093758"
FT DOMAIN 190..359
FT /note="tr-type G"
FT REGION 53..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..206
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 224..228
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 245..248
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 299..302
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 335..337
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 59..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 199..206
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 245..249
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 299..302
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 688 AA; 75718 MW; EF8B835E0EB5203C CRC64;
MSKIRVHEYA KKNNISSKDL MTKLKEMNIE VSNHMTMLED EVVNKLDNQY SAGAEKPSVA
DEFEVEEKVV RSKKNSNKNK KKGKANEDKR QDNFAGRQQT PIVETPDKIT FSGSLTVGDL
AKKLSKEPSE IIKKLFMLGI MATINQDLDK DTIELIATDY GIEVEEEVVV SETEFETFID
EQDDEENLKE RPAVVTIMGH VDHGKTTLLD SIRNSKVTAG EAGGITQHIG AYQVDVNDKK
ITFLDTPGHA VFTTMRARGA QVTDITILVV AADDGVMPQT VEAISHAKAA GVPIIVAVNK
MDKPAANPDR VMQELTEYEL VPEAWGGDTI FVPISAIQGE GIDNLLEMIL LVSEVEEYKA
NPNRYAAGTV IEAQLDKGKG TIATLLVQNG TLRVGDPIVV GTSFGRVRAM VSDIGRRVKV
AGPSTPVEIT GLNEVPQAGD RFMAFADEKK ARQIGESRAQ EALVAQRGEK SKFSLEDLFQ
QIQEGDVKEI NLIVKADVQG SVEAMAASLR KIDVEGVKVK IIHTGVGAIT ESDIILASAS
NAIVIGFNVR PDVNAKRTAE LEKVDVRLHR IIYKVIEEIE SAMQGMLDPE FEEKVIGQAE
VRQTFKVTKV GTIAGCYVID GKITRDSGVR IIRDGVVVFE GKLDTLKRFK DDVKEVAQNY
ECGITIERYN DLKEGDIIEA YVMEEVKR
