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UREG_YERE8
ID   UREG_YERE8              Reviewed;         221 AA.
AC   A1JKE2;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Urease accessory protein UreG {ECO:0000255|HAMAP-Rule:MF_01389};
GN   Name=ureG {ECO:0000255|HAMAP-Rule:MF_01389}; OrderedLocusNames=YE0956;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAL11054.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AM286415; CAL11054.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_004390399.1; NC_008800.1.
DR   RefSeq; YP_001005290.1; NC_008800.1.
DR   AlphaFoldDB; A1JKE2; -.
DR   SMR; A1JKE2; -.
DR   STRING; 393305.YE0956; -.
DR   EnsemblBacteria; CAL11054; CAL11054; YE0956.
DR   GeneID; 61904997; -.
DR   GeneID; 67420530; -.
DR   KEGG; yen:YE0956; -.
DR   PATRIC; fig|393305.7.peg.1057; -.
DR   eggNOG; COG0378; Bacteria.
DR   HOGENOM; CLU_072144_1_0_6; -.
DR   Proteomes; UP000000642; 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: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..221
FT                   /note="Urease accessory protein UreG"
FT                   /id="PRO_0000347457"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01389"
SQ   SEQUENCE   221 AA;  24182 MW;  1423E6D03E9E289F CRC64;
     MNSHSTDKRK KITRIGIGGP VGSGKTAIIE VITPILIKRG IKPLIITNDI VTTEDAKQVK
     RTLKGILDEE KILGVETGAC PHTAVREDPS MNIAAVEEME ERFPDSDLIM IESGGDNLTL
     TFSPALADFY IYVIDVAEGE KIPRKNGPGL VQADILVINK IDLAPYVGAS LDVMESDTKV
     VRGERPYILT NCKTGQGIEE LVDMIMRDFL FTHVQPQGEH A
 
 
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