ID   URE2_BORPE              Reviewed;         102 AA.
AC   Q7VUD2;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Urease subunit beta {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 {ECO:0000255|HAMAP-Rule:MF_01954};
GN   Name=ureB {ECO:0000255|HAMAP-Rule:MF_01954}; OrderedLocusNames=BP3169;
OS   Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257313;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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; BX640420; CAE43437.1; -; Genomic_DNA.
DR   RefSeq; NP_881731.1; NC_002929.2.
DR   RefSeq; WP_010931338.1; NZ_CP039022.1.
DR   AlphaFoldDB; Q7VUD2; -.
DR   SMR; Q7VUD2; -.
DR   STRING; 257313.BP3169; -.
DR   GeneID; 45387926; -.
DR   KEGG; bpe:BP3169; -.
DR   PATRIC; fig|257313.5.peg.3426; -.
DR   eggNOG; COG0832; Bacteria.
DR   HOGENOM; CLU_129707_1_1_4; -.
DR   OMA; FYEVNDA; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000002676; Chromosome.
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..102
FT                   /note="Urease subunit beta"
FT                   /id="PRO_0000234230"
SQ   SEQUENCE   102 AA;  11175 MW;  CB819BC440888573 CRC64;
     MIPGEILTEP GQIELNVGRP TLTIAVVNED DRPIQVGSHY HFAEANNALV FDRELATGYR
     LNIPAGNAVR FEPGMRRTVE LVAVGGERRI FGFQGKVMGA LK