ID   URE1_HELMU              Reviewed;         308 AA.
AC   P50045;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Urease subunit beta;
DE            EC=3.5.1.5;
DE   AltName: Full=Urea amidohydrolase subunit beta;
DE   Flags: Fragment;
GN   Name=ureB;
OS   Helicobacter mustelae.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NCTC 12032;
RX   PubMed=7642313; DOI=10.1128/iai.63.9.3718-3721.1995;
RA   Solnick J.V., Josenhans C., Tompkins L.S., Labigne A.;
RT   "Construction and characterization of an isogenic urease-negative mutant of
RT   Helicobacter mustelae.";
RL   Infect. Immun. 63:3718-3721(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|PROSITE-ProRule:PRU00700};
CC   -!- COFACTOR:
CC       Name=Ni cation; Xref=ChEBI:CHEBI:25516; Evidence={ECO:0000250};
CC       Note=Binds 2 nickel ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC       urea (urease route): step 1/1.
CC   -!- SUBUNIT: Heterohexamer of 3 UreA (alpha) and 3 UreB (beta) subunits.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00700}.
CC   -!- PTM: Carboxylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Urease alpha subunit family.
CC   -!- CAUTION: The orthologous protein is known as the alpha subunit (UreC)
CC       in most other bacteria. {ECO:0000305}.
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DR   EMBL; L33462; AAC41484.1; -; Genomic_DNA.
DR   AlphaFoldDB; P50045; -.
DR   SMR; P50045; -.
DR   MEROPS; M38.982; -.
DR   UniPathway; UPA00258; UER00370.
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-EC.
DR   GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.30.40.10; -; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR011612; Urease_alpha_N_dom.
DR   InterPro; IPR017951; Urease_asu_c.
DR   InterPro; IPR029754; Urease_Ni-bd.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF00449; Urease_alpha; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   PROSITE; PS01120; UREASE_1; 1.
DR   PROSITE; PS51368; UREASE_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Metal-binding; Nickel.
FT   CHAIN           1..>308
FT                   /note="Urease subunit beta"
FT                   /id="PRO_0000067532"
FT   DOMAIN          131..>308
FT                   /note="Urease"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00700"
FT   BINDING         136
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00700"
FT   BINDING         138
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00700"
FT   BINDING         219
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00700"
FT   BINDING         219
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00700"
FT   BINDING         248
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00700"
FT   BINDING         274
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00700"
FT   MOD_RES         219
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000250"
FT   NON_TER         308
SQ   SEQUENCE   308 AA;  32118 MW;  1F11F29A5B3C84B1 CRC64;
     MIKISRKEYV SMYGPTTGDK VRLGDTELIA EIEKDYTVYG EEIKFGGGKT IRDGMSQSVS
     PDVNELDAVI TNAMIIDYTG IYKADIGIKD GKIAGIGKAG NRDTQDGVGM DLVVGASTEA
     IAGEGLIVTA GGIDTHIHFI SPTQIPTALY SGVTTMIGGG TGPAAGTFAT TISPGEWNIK
     QMIRAAEEYT MNLGFFGKGN TSNVKALEDQ IKAGALGFKV HEDCGSTPAV INHSLDIAEK
     YDVQVAIHTD TLNEGGAVED TLAAIGGRTI HTFHTEGAGG GHAPDIIKAA GEANILPAST
     NPTIPFTK