URE2_PROMH
ID URE2_PROMH Reviewed; 108 AA.
AC P17087; B4EXN4;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 25-MAY-2022, entry version 138.
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=PMI3684;
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2687233; DOI=10.1128/jb.171.12.6414-6422.1989;
RA Jones B.D., Mobley H.L.T.;
RT "Proteus mirabilis urease: nucleotide sequence determination and comparison
RT with jack bean urease.";
RL J. Bacteriol. 171:6414-6422(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320;
RX PubMed=18375554; DOI=10.1128/jb.01981-07;
RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA Parkhill J., Mobley H.L.T.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(2008).
RN [3]
RP UREASE AS A VIRULENCE FACTOR.
RX PubMed=2180821; DOI=10.1128/iai.58.4.1120-1123.1990;
RA Jones B.D., Lockatell C.V., Johnson D.E., Warren J.W., Mobley H.L.T.;
RT "Construction of a urease-negative mutant of Proteus mirabilis: analysis of
RT virulence in a mouse model of ascending urinary tract infection.";
RL Infect. Immun. 58:1120-1123(1990).
RN [4]
RP CATALYTIC ACTIVITY.
RX PubMed=8500894; DOI=10.1128/iai.61.6.2570-2577.1993;
RA Sriwanthana B., Mobley H.L.T.;
RT "Proteus mirabilis urease: histidine 320 of UreC is essential for urea
RT hydrolysis and nickel ion binding within the native enzyme.";
RL Infect. Immun. 61:2570-2577(1993).
RN [5]
RP INDUCTION.
RX PubMed=7678244; DOI=10.1128/jb.175.2.465-473.1993;
RA Nicholson E.B., Concaugh E.A., Foxall P.A., Island M.D., Mobley H.L.T.;
RT "Proteus mirabilis urease: transcriptional regulation by UreR.";
RL J. Bacteriol. 175:465-473(1993).
RN [6]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF MET-1.
RX PubMed=7559355; DOI=10.1128/jb.177.19.5653-5660.1995;
RA Island M.D., Mobley H.L.T.;
RT "Proteus mirabilis urease: operon fusion and linker insertion analysis of
RT ure gene organization, regulation, and function.";
RL J. Bacteriol. 177:5653-5660(1995).
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:7559355, ECO:0000269|PubMed:8500894};
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: Probable heterotrimer of UreA (gamma), UreB (beta) and UreC
CC (alpha) subunits. Three heterotrimers associate to form the active
CC enzyme. The trimeric urease interacts with an accessory complex
CC composed of UreD, UreF and UreG, which is required for the assembly of
CC the nickel containing metallocenter of UreC. The UreE protein may also
CC play a direct role in nickel transfer to the urease apoprotein.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01954}.
CC -!- INDUCTION: By urea. {ECO:0000269|PubMed:7678244}.
CC -!- SIMILARITY: Belongs to the urease beta subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01954}.
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DR EMBL; M31834; AAA25668.1; -; Genomic_DNA.
DR EMBL; AM942759; CAR47183.1; -; Genomic_DNA.
DR PIR; C43719; C43719.
DR RefSeq; WP_012368847.1; NC_010554.1.
DR AlphaFoldDB; P17087; -.
DR SMR; P17087; -.
DR STRING; 529507.PMI3684; -.
DR EnsemblBacteria; CAR47183; CAR47183; PMI3684.
DR GeneID; 6801197; -.
DR KEGG; pmr:PMI3684; -.
DR PATRIC; fig|529507.6.peg.3605; -.
DR eggNOG; COG0832; Bacteria.
DR HOGENOM; CLU_129707_1_1_6; -.
DR OMA; FYEVNDA; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000008319; 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; Reference proteome; Virulence.
FT CHAIN 1..108
FT /note="Urease subunit beta"
FT /id="PRO_0000067582"
FT MUTAGEN 1
FT /note="M->MRRRI: Reduces activity 2.5-fold."
FT /evidence="ECO:0000269|PubMed:7559355"
FT CONFLICT 81
FT /note="V -> VD (in Ref. 1; AAA25668)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 108 AA; 12054 MW; D8A9590A168AEFE6 CRC64;
MIPGEIRVNA ALGDIELNAG RETKTIQVAN HGDRPVQVGS HYHFYEVNEA LRFARKETLG
FRLNIPAGMA VRFEPGQSRT VELVAFAGKR EIYGFHGKVM GKLESEKK
