URE2_STAS1
ID URE2_STAS1 Reviewed; 134 AA.
AC Q4A0J4;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 105.
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=SSP0264;
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
RN [2]
RP PROTEIN SEQUENCE OF 1-6, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=8042901; DOI=10.1007/bf00288948;
RA Schaefer U.K., Kaltwasser H.;
RT "Urease from Staphylococcus saprophyticus: purification, characterization
RT and comparison to Staphylococcus xylosus urease.";
RL Arch. Microbiol. 161:393-399(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 ECO:0000269|PubMed:8042901};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.5 mM for urea (at 37 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:8042901};
CC Vmax=1.979 mmol/min/mg enzyme {ECO:0000269|PubMed:8042901};
CC pH dependence:
CC Optimum pH is 7.0 in phosphate buffer. {ECO:0000269|PubMed:8042901};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:8042901};
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; AP008934; BAE17409.1; -; Genomic_DNA.
DR RefSeq; WP_011302250.1; NZ_MTGA01000037.1.
DR AlphaFoldDB; Q4A0J4; -.
DR SMR; Q4A0J4; -.
DR STRING; 342451.SSP0264; -.
DR EnsemblBacteria; BAE17409; BAE17409; SSP0264.
DR KEGG; ssp:SSP0264; -.
DR PATRIC; fig|342451.11.peg.267; -.
DR eggNOG; COG0832; Bacteria.
DR HOGENOM; CLU_129707_2_2_9; -.
DR OMA; FYEVNDA; -.
DR OrthoDB; 1755809at2; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000006371; 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; Direct protein sequencing; Hydrolase; Reference proteome.
FT CHAIN 1..134
FT /note="Urease subunit beta"
FT /id="PRO_0000234274"
SQ SEQUENCE 134 AA; 14930 MW; 1416F1E2CD62E495 CRC64;
MKPGEIIVKR TEIEVNQGHN ATILNVKNTG DRPIQVGSHY HFFEANPALQ FDHEKAYGKR
LDIPAGAAVR FEPGDEKEVQ LVEYSGKRKI YGFHGDVNGS IDESRVYKLE DDSTATEVIA
EQDKTSENAN KGRG