(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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