ID   URE2_STRE5              Reviewed;         103 AA.
AC   Q55054; F8HGK1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 2.
DT   03-AUG-2022, entry version 101.
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=Ssal_01901;
OS   Streptococcus salivarius (strain 57.I).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1046629;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=57.I;
RX   PubMed=8550211; DOI=10.1128/iai.64.2.585-592.1996;
RA   Chen Y.-Y.M., Clancy K.A., Burne R.A.;
RT   "Streptococcus salivarius urease: genetic and biochemical characterization
RT   and expression in a dental plaque streptococcus.";
RL   Infect. Immun. 64:585-592(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=57.I;
RX   PubMed=21914897; DOI=10.1128/jb.05670-11;
RA   Geng J., Huang S.C., Li S., Hu S., Chen Y.Y.;
RT   "Complete genome sequence of the ureolytic Streptococcus salivarius strain
RT   57.I.";
RL   J. Bacteriol. 193:5596-5597(2011).
RN   [3]
RP   INDUCTION.
RC   STRAIN=57.I;
RX   PubMed=8595861; DOI=10.1111/j.1574-6968.1996.tb07993.x;
RA   Chen Y.-Y.M., Burne R.A.;
RT   "Analysis of Streptococcus salivarius urease expression using continuous
RT   chemostat culture.";
RL   FEMS Microbiol. Lett. 135:223-229(1996).
RN   [4]
RP   INDUCTION.
RC   STRAIN=57.I;
RX   PubMed=9791132; DOI=10.1128/jb.180.21.5769-5775.1998;
RA   Chen Y.-Y.M., Weaver C.A., Mendelsohn D.R., Burne R.A.;
RT   "Transcriptional regulation of the Streptococcus salivarius 57.I urease
RT   operon.";
RL   J. Bacteriol. 180:5769-5775(1998).
RN   [5]
RP   FUNCTION.
RC   STRAIN=57.I;
RX   PubMed=10913107; DOI=10.1128/jb.182.16.4667-4669.2000;
RA   Chen Y.-Y.M., Weaver C.A., Burne R.A.;
RT   "Dual functions of Streptococcus salivarius urease.";
RL   J. Bacteriol. 182:4667-4669(2000).
CC   -!- FUNCTION: Ureolysis may allow urea to be employed as a nitrogen source
CC       for growth and produces ammonia which may protect from killing at low
CC       pH. {ECO:0000269|PubMed:10913107}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.7 mM for urea (at pH 7.0 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:8550211};
CC         Note=Urea concentrations in the oral cavity of humans normally range
CC         from 3 mM to 10 mM.;
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|PubMed:8550211};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius.
CC         {ECO:0000269|PubMed:8550211};
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   -!- INDUCTION: By low pH and excess glucose. {ECO:0000269|PubMed:8595861,
CC       ECO:0000269|PubMed:9791132}.
CC   -!- SIMILARITY: Belongs to the urease beta subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01954}.
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DR   EMBL; U35248; AAC43563.1; -; Genomic_DNA.
DR   EMBL; CP002888; AEJ54137.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q55054; -.
DR   SMR; Q55054; -.
DR   STRING; 1046629.Ssal_01901; -.
DR   EnsemblBacteria; AEJ54137; AEJ54137; Ssal_01901.
DR   KEGG; stf:Ssal_01901; -.
DR   PATRIC; fig|1046629.4.peg.1687; -.
DR   eggNOG; COG0832; Bacteria.
DR   OMA; FYEVNDA; -.
DR   BioCyc; MetaCyc:MON-183; -.
DR   SABIO-RK; Q55054; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000000293; 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   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase.
FT   CHAIN           1..103
FT                   /note="Urease subunit beta"
FT                   /id="PRO_0000067596"
FT   CONFLICT        48
FT                   /note="A -> S (in Ref. 1; AAC43563)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   103 AA;  11478 MW;  7C630CA2542B3F4F CRC64;
     MIPGEYHVAS EPIDYNGGYE AISLEVKNVG DRAAQVGSHY HFYEANEAGL QFDREKARGK
     RLDIPAGTAI RFEPGETKTV QLIDFGGKRR IFGFNNKVNG FLD