IF2_BACCN
ID IF2_BACCN Reviewed; 689 AA.
AC A7GRE3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, 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=Bcer98_2465;
OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315749;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98;
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; CP000764; ABS22701.1; -; Genomic_DNA.
DR RefSeq; WP_012094905.1; NC_009674.1.
DR AlphaFoldDB; A7GRE3; -.
DR SMR; A7GRE3; -.
DR STRING; 315749.Bcer98_2465; -.
DR EnsemblBacteria; ABS22701; ABS22701; Bcer98_2465.
DR GeneID; 56418005; -.
DR KEGG; bcy:Bcer98_2465; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002300; 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..689
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000075592"
FT DOMAIN 191..360
FT /note="tr-type G"
FT REGION 70..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..207
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 225..229
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 246..249
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 300..303
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 336..338
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 92..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 200..207
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 246..250
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 300..303
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 689 AA; 76011 MW; 93EBC3B4458C6AE7 CRC64;
MSKIRVYEYA KKYNISSKEI ITKLKEMNIE VSNHMTMLDD EVVNKLDNEY NNEVKKPSVA
DEFEVEEKVV RSKKNSNKKK KKGKGNQDKR QENFAGKQQA QTVETPDKIT FSGTLTVGEL
ANKLGKEPSE IIKKLFMLGI MATINQDLDK DTIELIASDY GIEVEEEVVI DEIEFETFID
EQDEEEGDLK ERPAVVTIMG HVDHGKTTLL DSIRNSKVTA GEAGGITQHI GAYQVEVNDK
KITFLDTPGH AAFTTMRARG AQVTDITILV VAADDGVMPQ TVEAINHAKA AGVPIIVAVN
KMDKPAANPD RVMQELTEYE LVPEAWGGDT IFVPISAIKG EGIDNLLEMI LLVSEVEEYK
ANPNRYATGT VIEAQLDKGK GAIATLLVQN GTLRVGDPIV VGTTYGRVRA MVNDIGRRVK
VAGPSTPVEI TGLNEVPQAG DRFMAFADEK KARQIGESRA QQALLAQRGE KSKLSLEDLF
QQIQEGDVKE INLIVKADVQ GSVEAMAASL RKIDVEGVKV KIIHTGVGAI TESDIILASA
SNAIVIGFNV RPDVNAKRTA ESENVDIRLH RIIYKAIEEI EAAMRGMLDP EFEEKVIGQA
EVRQTFKVTK VGTIAGCYVT DGKITRDSGV RIIRDGVVIY EGQLDTLKRF KDDVKEVAQN
YECGITIEKY NDIKEGDIIE AFIMEEVKR
