URE3_STRE5
ID URE3_STRE5 Reviewed; 100 AA.
AC Q55053; F8HGK2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Urease subunit gamma {ECO:0000255|HAMAP-Rule:MF_00739};
DE EC=3.5.1.5 {ECO:0000255|HAMAP-Rule:MF_00739};
DE AltName: Full=Urea amidohydrolase subunit gamma {ECO:0000255|HAMAP-Rule:MF_00739};
GN Name=ureA {ECO:0000255|HAMAP-Rule:MF_00739}; OrderedLocusNames=Ssal_01902;
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_00739};
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_00739}.
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_00739}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00739}.
CC -!- INDUCTION: By low pH and excess glucose. {ECO:0000269|PubMed:8595861,
CC ECO:0000269|PubMed:9791132}.
CC -!- SIMILARITY: Belongs to the urease gamma subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_00739}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEJ54138.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U35248; AAC43562.1; -; Genomic_DNA.
DR EMBL; CP002888; AEJ54138.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q55053; -.
DR SMR; Q55053; -.
DR STRING; 1046629.Ssal_01902; -.
DR EnsemblBacteria; AEJ54138; AEJ54138; Ssal_01902.
DR KEGG; stf:Ssal_01902; -.
DR PATRIC; fig|1046629.4.peg.1688; -.
DR eggNOG; COG0831; Bacteria.
DR BioCyc; MetaCyc:MON-184; -.
DR SABIO-RK; Q55053; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000000293; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016151; F:nickel cation binding; 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; cd00390; Urease_gamma; 1.
DR Gene3D; 3.30.280.10; -; 1.
DR HAMAP; MF_00739; Urease_gamma; 1.
DR InterPro; IPR012010; Urease_gamma.
DR InterPro; IPR002026; Urease_gamma/gamma-beta_su.
DR InterPro; IPR036463; Urease_gamma_sf.
DR Pfam; PF00547; Urease_gamma; 1.
DR PIRSF; PIRSF001223; Urease_gamma; 1.
DR SUPFAM; SSF54111; SSF54111; 1.
DR TIGRFAMs; TIGR00193; urease_gam; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase.
FT CHAIN 1..100
FT /note="Urease subunit gamma"
FT /id="PRO_0000098050"
FT CONFLICT 9
FT /note="E -> K (in Ref. 1; AAC43562)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 100 AA; 11299 MW; 8F7A87B354FABF7B CRC64;
MQLTMREQEK MMISLAAMIA QRRKDKGIKL NHPEAVALIT DYVLEGAREG KTVAQLMDEA
RNLLTREDVM EGIAEMIPMI QVEATFTDST KLVTVHDPIQ
