ID   URE2_STAXY              Reviewed;         137 AA.
AC   P42874;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 102.
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};
OS   Staphylococcus xylosus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1288;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-6.
RC   STRAIN=DSM 20267 / Isolate C2A;
RX   PubMed=8042900; DOI=10.1007/bf00288947;
RA   Jose J., Schaefer U.K., Kaltwasser H.;
RT   "Threonine is present instead of cysteine at the active site of urease from
RT   Staphylococcus xylosus.";
RL   Arch. Microbiol. 161:384-392(1994).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X74600; CAA52679.1; -; Genomic_DNA.
DR   PIR; S38484; S38484.
DR   RefSeq; WP_042361935.1; NZ_VBTJ01000002.1.
DR   AlphaFoldDB; P42874; -.
DR   SMR; P42874; -.
DR   STRING; 1288.SXYLSMQ121_0291; -.
DR   GeneID; 45495930; -.
DR   eggNOG; COG0832; Bacteria.
DR   OrthoDB; 1755809at2; -.
DR   UniPathway; UPA00258; UER00370.
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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Hydrolase.
FT   CHAIN           1..137
FT                   /note="Urease subunit beta"
FT                   /id="PRO_0000067595"
FT   REGION          118..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   137 AA;  15432 MW;  AC6E869B8CB7067C CRC64;
     MKPGEIIVKR TEIEVNRGHN ATILDVKNTG DRPIQVGSHY HFFEANPALQ FEREKAYGKR
     LDIPAGAAVR FEPGDEKEVQ LVEYSGKRRI FGFHGEVNGP IDEARVYKAE DDDSATEIIA
     EENKVSENAN KESGYNR