URE22_BRUA2
ID URE22_BRUA2 Reviewed; 159 AA.
AC Q2YQD9;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Urease subunit beta 2 {ECO:0000255|HAMAP-Rule:MF_01954};
DE EC=3.5.1.5 {ECO:0000255|HAMAP-Rule:MF_01954};
DE AltName: Full=Urea amidohydrolase subunit beta 2 {ECO:0000255|HAMAP-Rule:MF_01954};
GN Name=ureB2 {ECO:0000255|HAMAP-Rule:MF_01954}; OrderedLocusNames=BAB1_1377;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; 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 assessment
RT 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 activity
CC or pathogen survival in BALB/c mice when administered orally.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+); Xref=Rhea:RHEA:20557,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.5;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01954};
CC -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC urea (urease route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01954}.
CC -!- SUBUNIT: Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha)
CC subunits. Three heterotrimers associate to form the active enzyme.
CC {ECO:0000255|HAMAP-Rule:MF_01954}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01954}.
CC -!- SIMILARITY: Belongs to the urease beta subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01954}.
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DR EMBL; AM040264; CAJ11333.1; -; Genomic_DNA.
DR RefSeq; WP_002964470.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YQD9; -.
DR SMR; Q2YQD9; -.
DR STRING; 359391.BAB1_1377; -.
DR EnsemblBacteria; CAJ11333; CAJ11333; BAB1_1377.
DR GeneID; 3787946; -.
DR KEGG; bmf:BAB1_1377; -.
DR PATRIC; fig|359391.11.peg.827; -.
DR HOGENOM; CLU_129707_2_0_5; -.
DR OMA; VVHNTGD; -.
DR PhylomeDB; Q2YQD9; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000002719; Chromosome I.
DR GO; GO:0035550; C:urease complex; IEA:InterPro.
DR GO; GO:0009039; F:urease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00407; Urease_beta; 1.
DR Gene3D; 2.10.150.10; -; 1.
DR HAMAP; MF_01954; Urease_beta; 1.
DR InterPro; IPR002019; Urease_beta.
DR InterPro; IPR036461; Urease_betasu_sf.
DR Pfam; PF00699; Urease_beta; 1.
DR SUPFAM; SSF51278; SSF51278; 1.
DR TIGRFAMs; TIGR00192; urease_beta; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..159
FT /note="Urease subunit beta 2"
FT /id="PRO_0000234235"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 159 AA; 17763 MW; 780EDDB24A15DF16 CRC64;
MAKEPTEAAH PQPEQTKTNH KAHRPVGGYV LAKDPIEINQ GRPRTTLTVR NTGDRPIQIG
SHFHFFEVNR YLEFDRSKAF GLRLDIPANT AVRFEPGDEK EVTLVPFAGK RFIFGFNNLV
DGWSGDGPTP DYQPNREIAA ERAEKLGFKS CKSGGKDAK