ID   URE2_SYNPV              Reviewed;         106 AA.
AC   O87401;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 88.
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   Synechococcus sp. (strain WH7805).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=59931;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=10075427; DOI=10.1099/13500872-145-2-447;
RA   Collier J.L., Brahamsha B., Palenik B.;
RT   "The marine cyanobacterium Synechococcus sp. WH7805 requires urease (urea
RT   amidohydrolase, EC 3.5.1.5) to utilize urea as a nitrogen source:
RT   molecular-genetic and biochemical analysis of the enzyme.";
RL   Microbiology 145:447-459(1999).
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:10075427};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.232 mM for urea {ECO:0000269|PubMed:10075427};
CC         Vmax=0.0013 mmol/min/mg enzyme {ECO:0000269|PubMed:10075427};
CC       pH dependence:
CC         Optimum pH is 8.6. {ECO:0000269|PubMed:10075427};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius.
CC         {ECO:0000269|PubMed:10075427};
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; AF056189; AAC61501.1; -; Genomic_DNA.
DR   RefSeq; WP_006042763.1; NZ_CH724168.1.
DR   AlphaFoldDB; O87401; -.
DR   SMR; O87401; -.
DR   STRING; 59931.WH7805_09814; -.
DR   eggNOG; COG0832; Bacteria.
DR   OMA; FYEVNDA; -.
DR   PhylomeDB; O87401; -.
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; Hydrolase.
FT   CHAIN           1..106
FT                   /note="Urease subunit beta"
FT                   /id="PRO_0000234280"
SQ   SEQUENCE   106 AA;  11298 MW;  88D28D2BBCCA1671 CRC64;
     MAPFIPGELL PEPGEIELNA GRPVTSLHVA NSGDRPVQVG SHFHFAEANA ALQFDRTAAR
     GQRLDIPAGT AIRFEPGDSR DVNLIPFAGD RRVIGFNGQI NGPLDA