ID   URE3_MYCBP              Reviewed;         100 AA.
AC   A1KJR0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=BCG_1884;
OS   Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=410289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Pasteur 1173P2;
RX   PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA   Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA   Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA   Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA   Barrell B.G., Parkhill J., Cole S.T.;
RT   "Genome plasticity of BCG and impact on vaccine efficacy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
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   -!- 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   -!- SIMILARITY: Belongs to the urease gamma subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_00739}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM408590; CAL71871.1; -; Genomic_DNA.
DR   RefSeq; WP_003409305.1; NC_008769.1.
DR   AlphaFoldDB; A1KJR0; -.
DR   SMR; A1KJR0; -.
DR   KEGG; mbb:BCG_1884; -.
DR   HOGENOM; CLU_145825_1_0_11; -.
DR   OMA; MQLTPHE; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000001472; 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   3: Inferred from homology;
KW   Cytoplasm; Hydrolase.
FT   CHAIN           1..100
FT                   /note="Urease subunit gamma"
FT                   /id="PRO_1000046337"
SQ   SEQUENCE   100 AA;  11090 MW;  D603C57309AC6507 CRC64;
     MRLTPHEQER LLLSYAAELA RRRRARGLRL NHPEAIAVIA DHILEGARDG RTVAELMASG
     REVLGRDDVM EGVPEMLAEV QVEATFPDGT KLVTVHQPIA