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Database: UniProt
Entry: URE12_BRUA2
LinkDB: URE12_BRUA2
Original site: URE12_BRUA2 
ID   URE12_BRUA2             Reviewed;         573 AA.
AC   Q2YQD8;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   16-OCT-2019, entry version 86.
DE   RecName: Full=Urease subunit alpha 2 {ECO:0000255|HAMAP-Rule:MF_01953};
DE            EC=3.5.1.5 {ECO:0000255|HAMAP-Rule:MF_01953};
DE   AltName: Full=Urea amidohydrolase subunit alpha 2 {ECO:0000255|HAMAP-Rule:MF_01953};
GN   Name=ureC2 {ECO:0000255|HAMAP-Rule:MF_01953};
GN   OrderedLocusNames=BAB1_1378;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
RN   [2]
RP   LACK OF ROLE IN VIRULENCE.
RX   PubMed=17101645; DOI=10.1128/iai.01244-06;
RA   Sangari F.J., Seoane A., Rodriguez M.C., Aguero J., Garcia Lobo J.M.;
RT   "Characterization of the urease operon of Brucella abortus and
RT   assessment of its role in virulence of the bacterium.";
RL   Infect. Immun. 75:774-780(2007).
CC   -!- FUNCTION: Disrupting the ure2 operon has no effect on urease
CC       activity or pathogen survival in BALB/c mice when administered
CC       orally.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+);
CC         Xref=Rhea:RHEA:20557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16199, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938;
CC         EC=3.5.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_01953};
CC   -!- COFACTOR:
CC       Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01953};
CC       Note=Binds 2 nickel ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01953};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3)
CC       from urea (urease route): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01953}.
CC   -!- SUBUNIT: Heterotrimer of UreA (gamma), UreB (beta) and UreC
CC       (alpha) subunits. Three heterotrimers associate to form the active
CC       enzyme. {ECO:0000255|HAMAP-Rule:MF_01953}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01953}.
CC   -!- PTM: Carboxylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000255|HAMAP-Rule:MF_01953}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. Urease alpha subunit family. {ECO:0000255|HAMAP-
CC       Rule:MF_01953}.
DR   EMBL; AM040264; CAJ11334.1; -; Genomic_DNA.
DR   RefSeq; WP_002966881.1; NZ_KN046823.1.
DR   SMR; Q2YQD8; -.
DR   PRIDE; Q2YQD8; -.
DR   EnsemblBacteria; CAJ11334; CAJ11334; BAB1_1378.
DR   KEGG; bmf:BAB1_1378; -.
DR   PATRIC; fig|359391.11.peg.828; -.
DR   HOGENOM; HOG000075064; -.
DR   KO; K01428; -.
DR   OMA; CHHLSHD; -.
DR   BioCyc; BABO359391:G1GJA-1403-MONOMER; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000002719; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009039; F:urease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00375; Urease_alpha; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   HAMAP; MF_01953; Urease_alpha; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR011612; Urease_alpha_N_dom.
DR   InterPro; IPR017950; Urease_AS.
DR   InterPro; IPR005848; Urease_asu.
DR   InterPro; IPR017951; Urease_asu_c.
DR   InterPro; IPR029754; Urease_Ni-bd.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF00449; Urease_alpha; 1.
DR   PRINTS; PR01752; UREASE.
DR   SUPFAM; SSF51338; SSF51338; 2.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR01792; urease_alph; 1.
DR   PROSITE; PS01120; UREASE_1; 1.
DR   PROSITE; PS00145; UREASE_2; 1.
DR   PROSITE; PS51368; UREASE_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Nickel;
KW   Reference proteome.
FT   CHAIN         1    573       Urease subunit alpha 2.
FT                                /FTId=PRO_0000234142.
FT   DOMAIN      135    573       Urease. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   ACT_SITE    326    326       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   METAL       140    140       Nickel 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       142    142       Nickel 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       223    223       Nickel 1; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       223    223       Nickel 2; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       252    252       Nickel 2; via pros nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       278    278       Nickel 2; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       366    366       Nickel 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   BINDING     225    225       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   MOD_RES     223    223       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
SQ   SEQUENCE   573 AA;  60738 MW;  C9A71703FF500BF6 CRC64;
     MTQISRQQYA DLYGPTIGDK IRLGDSDLYV EIEKDLRATY GDELQYGGGK TLRDGMGSEN
     FLTQEAGCLD LVITNVTVID AIQGVVKADV GIRNGRIVGL GKAGNPSTKD GVTRGLVTGA
     STDAISGEHL ILTAGGMDTH VHYIAPQQVE AALSNGITTL WGGGIGPVDG TNGVTTTNGP
     WNLEMMLRSI EGLPINFGIQ GKGNSTGIAP LIEQLEAGAA GFKVHEDYGA TPATIRACLS
     VADEYDVSVA VHTDTLNESG YVEDTIAAFD GRSVHTYHSE GAGGGHAPDL LKVVGQNNIL
     PSSTNPTLPC GKNSVAELFD MIMVCHNLNP KIPSDVAFAE SRVRAETIVA ESVLHDMGAI
     SMIGSDSQAM GRLGETFLRA IQTADAMKKA RGPLPEDAPG NDNFRVLRYI AKVTINPALT
     AGVGDVIGSI ESGKFADLVL WEPAFFGVKP KLVLKGGLVA WANMGDPNAS LPTPQPMYYR
     PMFAAYGSAL QKTSITFVSR AAYDKGVADR FGLQRLVMPV SGTRVIGKAH MVRNSYLPNI
     EVDPQTFAVK VDGVHATVKP PQSISLNQLY FFS
//
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