IF2_BACCZ
ID IF2_BACCZ Reviewed; 686 AA.
AC Q636L3;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BCE33L3572;
OS Bacillus cereus (strain ZK / E33L).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=288681;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZK / E33L;
RX PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(2006).
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; CP000001; AAU16695.1; -; Genomic_DNA.
DR RefSeq; WP_000036341.1; NZ_CP009968.1.
DR AlphaFoldDB; Q636L3; -.
DR SMR; Q636L3; -.
DR EnsemblBacteria; AAU16695; AAU16695; BCE33L3572.
DR KEGG; bcz:BCE33L3572; -.
DR PATRIC; fig|288681.22.peg.1839; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000002612; 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..686
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228164"
FT DOMAIN 188..357
FT /note="tr-type G"
FT REGION 54..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..204
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 222..226
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 243..246
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 297..300
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 333..335
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 54..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 197..204
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 243..247
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 297..300
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 686 AA; 75724 MW; BCC45740327CACAC CRC64;
MSKIRVHEYA KKHNISSKDL MTKLKEMNIE VSNHMTMLDD EVVNKLDNEY QAEKPSVADE
FEVEEKVVRS KKNSNKKKKK GKGNEDKRQE NFAGRQQTQT VETPDKITFS GSLTVGDLAK
KLSKEPSEII KKLFMLGIMA TINQDLDKDT IELIANDYGI EVEEEVIVSE TEFETFIDEQ
DDEENLKERP AVVTIMGHVD HGKTTLLDSI RNSKVTAGEA GGITQHIGAY QVEVNDKKIT
FLDTPGHAAF TTMRARGAQV TDITILVVAA DDGVMPQTVE AINHAKAAGV PIIVAVNKMD
KPAANPDRVM QELTEYELVP EAWGGDTIFV PISAIQGEGI DNLLEMILLV SEVEEYKANP
NRYATGTVIE AQLDKGKGTI ATLLVQNGTL RVGDPIVVGT SFGRVRAMVS DIGRRVKVAG
PSTPVEITGL NEVPQAGDRF MAFADEKKAR QIGESRAQEA LLAQRGEKSK LSLEDLFQQI
QEGDVKEINL IVKADVQGSV EAMAASLRKI DVEGVKVKII HTGVGAITES DIILASASNA
IVIGFNVRPD VNAKRTAELE NVDIRLHRII YKVIEEIEAA MQGMLDPEFE EKVIGQAEVR
QTFKVTKVGT IAGCYVTDGK ITRDSGVRII RDGVVIFEGQ LDTLKRFKDD VKEVAQNYEC
GITIERYNDL KEGDIIEAYI MEEVKR
