ID   URE2_MYCTU              Reviewed;         104 AA.
AC   P9WFE9; L0TAK7; P0A662; P50048;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 36.
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=Rv1849;
GN   ORFNames=MTCY359.24c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-5, CATALYTIC
RP   ACTIVITY, INTERACTION WITH UREA AND UREC, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=7559354; DOI=10.1128/jb.177.19.5644-5652.1995;
RA   Clemens D.L., Lee B.-Y., Horwitz M.A.;
RT   "Purification, characterization, and genetic analysis of Mycobacterium
RT   tuberculosis urease, a potentially critical determinant of host-pathogen
RT   interaction.";
RL   J. Bacteriol. 177:5644-5652(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=7568014; DOI=10.1073/pnas.92.19.8768;
RA   Reyrat J.-M., Berthet F.-X., Gicquel B.;
RT   "The urease locus of Mycobacterium tuberculosis and its utilization for the
RT   demonstration of allelic exchange in Mycobacterium bovis bacillus Calmette-
RT   Guerin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:8768-8772(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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:7559354};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.3 mM for urea {ECO:0000269|PubMed:7559354};
CC         Vmax=0.05 mmol/min/mg enzyme {ECO:0000269|PubMed:7559354};
CC       pH dependence:
CC         Optimum pH is 7.2. {ECO:0000269|PubMed:7559354};
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   -!- 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; U33011; AAC43474.1; -; Genomic_DNA.
DR   EMBL; L41141; AAC37006.1; -; Genomic_DNA.
DR   EMBL; AL123456; CCP44615.1; -; Genomic_DNA.
DR   PIR; A70665; A70665.
DR   RefSeq; NP_216365.1; NC_000962.3.
DR   RefSeq; WP_003409308.1; NZ_NVQJ01000013.1.
DR   AlphaFoldDB; P9WFE9; -.
DR   SMR; P9WFE9; -.
DR   STRING; 83332.Rv1849; -.
DR   PaxDb; P9WFE9; -.
DR   DNASU; 885710; -.
DR   GeneID; 45425822; -.
DR   GeneID; 885710; -.
DR   KEGG; mtu:Rv1849; -.
DR   TubercuList; Rv1849; -.
DR   eggNOG; COG0832; Bacteria.
DR   OMA; FYEVNDA; -.
DR   PhylomeDB; P9WFE9; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000001584; 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..104
FT                   /note="Urease subunit beta"
FT                   /id="PRO_0000067579"
SQ   SEQUENCE   104 AA;  11190 MW;  D621CE43A47304E0 CRC64;
     MIPGEIFYGS GDIEMNAAAL SRLQMRIINA GDRPVQVGSH VHLPQANRAL SFDRATAHGY
     RLDIPAATAV RFEPGIPQIV GLVPLGGRRE VPGLTLNPPG RLDR