(data stored in ACNUC1104 zone)

SWISSPROT: C0ZM24_RHOE4

ID   C0ZM24_RHOE4            Unreviewed;       213 AA.
AC   C0ZM24;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   08-MAY-2019, entry version 71.
DE   RecName: Full=Urease accessory protein UreG {ECO:0000256|HAMAP-Rule:MF_01389};
GN   Name=ureG {ECO:0000256|HAMAP-Rule:MF_01389,
GN   ECO:0000313|EMBL:BAH31001.1};
GN   OrderedLocusNames=RER_02930 {ECO:0000313|EMBL:BAH31001.1};
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH31001.1, ECO:0000313|Proteomes:UP000002204};
RN   [1] {ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAH31001.1, ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX   PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA   Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA   Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA   Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT   "Sequence analysis of three plasmids harboured in Rhodococcus
RT   erythropolis strain PR4.";
RL   Environ. Microbiol. 8:334-346(2006).
CC   -!- FUNCTION: Facilitates the functional incorporation of the urease
CC       nickel metallocenter. This process requires GTP hydrolysis,
CC       probably effectuated by UreG. {ECO:0000256|HAMAP-Rule:MF_01389,
CC       ECO:0000256|SAAS:SAAS00089878}.
CC   -!- SUBUNIT: Homodimer. UreD, UreF and UreG form a complex that acts
CC       as a GTP-hydrolysis-dependent molecular chaperone, activating the
CC       urease apoprotein by helping to assemble the nickel containing
CC       metallocenter of UreC. The UreE protein probably delivers the
CC       nickel. {ECO:0000256|HAMAP-Rule:MF_01389}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01389,
CC       ECO:0000256|SAAS:SAAS00089883}.
CC   -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. UreG
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01389,
CC       ECO:0000256|SAAS:SAAS00571589}.
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DR   EMBL; AP008957; BAH31001.1; -; Genomic_DNA.
DR   RefSeq; WP_007731713.1; NC_012490.1.
DR   STRING; 234621.RER_02930; -.
DR   EnsemblBacteria; BAH31001; BAH31001; RER_02930.
DR   GeneID; 31540160; -.
DR   KEGG; rer:RER_02930; -.
DR   PATRIC; fig|234621.6.peg.728; -.
DR   eggNOG; ENOG4107S16; Bacteria.
DR   eggNOG; COG0378; LUCA.
DR   HOGENOM; HOG000236979; -.
DR   KO; K03189; -.
DR   OMA; GEKMPRK; -.
DR   Proteomes; UP000002204; 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   HAMAP; MF_01389; UreG; 1.
DR   InterPro; IPR003495; CobW/HypB/UreG_dom.
DR   InterPro; IPR012202; NiFe-hyd/urease_mat_GTPase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004400; UreG.
DR   PANTHER; PTHR31715; PTHR31715; 1.
DR   Pfam; PF02492; cobW; 1.
DR   PIRSF; PIRSF005624; Ni-bind_GTPase; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00101; ureG; 1.
PE   3: Inferred from homology;
DR   PRODOM; C0ZM24.
DR   SWISS-2DPAGE; C0ZM24.
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_01389,
KW   ECO:0000256|SAAS:SAAS00462102};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002204};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01389,
KW   ECO:0000256|SAAS:SAAS00462084};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_01389,
KW   ECO:0000256|SAAS:SAAS01001112};
KW   Nickel insertion {ECO:0000256|HAMAP-Rule:MF_01389,
KW   ECO:0000256|SAAS:SAAS00462079};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01389,
KW   ECO:0000256|SAAS:SAAS01001115}.
FT   DOMAIN        7    180       cobW. {ECO:0000259|Pfam:PF02492}.
FT   NP_BIND      11     18       GTP. {ECO:0000256|HAMAP-Rule:MF_01389}.
SQ   SEQUENCE   213 AA;  22761 MW;  AE23CBE419E65FB5 CRC64;
     MKKTTRIGIG GPVGSGKTAL IEAITPEFIK RGTSVLIITN DVVTTEDAKH VRKALKGVLV
     EERIVGVETG ACPHTAVRED PSMNLAAVED MEKTFPDTDV VFIESGGDNL TLTFSPALVD
     FFIYVIDVAA GDKIPRKNGP GISQSDILVI NKTDLAPYVN ADLGVMDRDS KGMRGDKPFV
     FTNCMTGEGI KEVVDLIVHG VLFDEEEVGA SAP
//

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