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UREG1_BRUC2
ID   UREG1_BRUC2             Reviewed;         208 AA.
AC   A9M7V8;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Urease accessory protein UreG 1 {ECO:0000255|HAMAP-Rule:MF_01389};
GN   Name=ureG1 {ECO:0000255|HAMAP-Rule:MF_01389}; OrderedLocusNames=BCAN_A0276;
OS   Brucella canis (strain ATCC 23365 / NCTC 10854).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=483179;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23365 / NCTC 10854;
RA   Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA   Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA   Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA   Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA   Bruce D., Detter C., Munk C., Brettin T.S.;
RT   "Brucella canis ATCC 23365 whole genome shotgun sequencing project.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Facilitates the functional incorporation of the urease nickel
CC       metallocenter. This process requires GTP hydrolysis, probably
CC       effectuated by UreG. {ECO:0000255|HAMAP-Rule:MF_01389}.
CC   -!- SUBUNIT: Homodimer. UreD, UreF and UreG form a complex that acts as a
CC       GTP-hydrolysis-dependent molecular chaperone, activating the urease
CC       apoprotein by helping to assemble the nickel containing metallocenter
CC       of UreC. The UreE protein probably delivers the nickel.
CC       {ECO:0000255|HAMAP-Rule:MF_01389}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01389}.
CC   -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. UreG
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01389}.
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DR   EMBL; CP000872; ABX61368.1; -; Genomic_DNA.
DR   RefSeq; WP_002963437.1; NC_010103.1.
DR   AlphaFoldDB; A9M7V8; -.
DR   SMR; A9M7V8; -.
DR   EnsemblBacteria; ABX61368; ABX61368; BCAN_A0276.
DR   GeneID; 45051406; -.
DR   GeneID; 55590052; -.
DR   KEGG; bcs:BCAN_A0276; -.
DR   HOGENOM; CLU_072144_1_0_5; -.
DR   OMA; VDLTIYV; -.
DR   PhylomeDB; A9M7V8; -.
DR   Proteomes; UP000001385; Chromosome I.
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:InterPro.
DR   GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01389; UreG; 1.
DR   InterPro; IPR003495; CobW/HypB/UreG_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004400; UreG.
DR   PANTHER; PTHR31715; PTHR31715; 1.
DR   Pfam; PF02492; cobW; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00101; ureG; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; GTP-binding; Nickel insertion; Nucleotide-binding.
FT   CHAIN           1..208
FT                   /note="Urease accessory protein UreG 1"
FT                   /id="PRO_0000347358"
FT   BINDING         11..18
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01389"
SQ   SEQUENCE   208 AA;  22705 MW;  39FF82812CA4FDE2 CRC64;
     MTQKNGPLRV GIGGPVGSGK TTLTEKLCKA MRDKYSVAVI TNDIYTQEDA LILARRQALS
     EDRIIGVETG GCPHTAIRED ASINLQAVVE MTRRFPDLDV VFIESGGDNL AATFSPDLAD
     LTLYVISVCQ GEEIPRKGGP GITRSDFLVI NKSDLAPYVH VDLEVMEADA MRMRAKRPFG
     FTDLHRGKGV QEIIDFIVEN GGLEPRSN
 
 
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