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Database: UniProt
Entry: C3GMR6_BACTU
LinkDB: C3GMR6_BACTU
Original site: C3GMR6_BACTU 
ID   C3GMR6_BACTU            Unreviewed;       686 AA.
AC   C3GMR6;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000256|HAMAP-Rule:MF_00100};
GN   ORFNames=bthur0010_35530 {ECO:0000313|EMBL:EEM76273.1};
OS   Bacillus thuringiensis serovar pondicheriensis BGSC 4BA1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=527029 {ECO:0000313|EMBL:EEM76273.1};
RN   [1] {ECO:0000313|EMBL:EEM76273.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGSC 4BA1 {ECO:0000313|EMBL:EEM76273.1};
RX   PubMed=22645259; DOI=10.1101/gr.134437.111;
RA   Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA   Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA   Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT   "Genomic characterization of the Bacillus cereus sensu lato species:
RT   Backdrop to the evolution of Bacillus anthracis.";
RL   Genome Res. 22:1512-1524(2012).
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:0000256|ARBA:ARBA00025162, ECO:0000256|HAMAP-
CC       Rule:MF_00100, ECO:0000256|RuleBase:RU000644}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|ARBA:ARBA00007733, ECO:0000256|HAMAP-Rule:MF_00100,
CC       ECO:0000256|RuleBase:RU000644}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEM76273.1}.
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DR   EMBL; ACNH01000068; EEM76273.1; -; Genomic_DNA.
DR   RefSeq; WP_000036341.1; NZ_CM000755.1.
DR   AlphaFoldDB; C3GMR6; -.
DR   SMR; C3GMR6; -.
DR   HOGENOM; CLU_006301_5_1_9; -.
DR   Proteomes; UP000006660; 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; cd01887; IF2_eIF5B; 1.
DR   CDD; cd03702; IF2_mtIF2_II; 1.
DR   CDD; cd03692; mtIF2_IVc; 1.
DR   Gene3D; 1.10.10.2480; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 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   NCBIfam; TIGR00487; IF-2; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43381:SF5; TRANSLATION INITIATION FACTOR IF-2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   Pfam; PF04760; IF2_N; 2.
DR   SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 2.
DR   PROSITE; PS51722; G_TR_2; 1.
DR   PROSITE; PS01176; IF2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00100};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW   Rule:MF_00100};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00100};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00100}.
FT   DOMAIN          188..357
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          54..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          191..339
FT                   /note="G-domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
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:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         243..247
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         297..300
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|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
//
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