URE1_HELHP
ID URE1_HELHP Reviewed; 569 AA.
AC Q93PJ4; Q7BYA2;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Urease subunit beta {ECO:0000255|HAMAP-Rule:MF_01953};
DE EC=3.5.1.5 {ECO:0000255|HAMAP-Rule:MF_01953};
DE AltName: Full=Urea amidohydrolase subunit beta {ECO:0000255|HAMAP-Rule:MF_01953};
GN Name=ureB {ECO:0000255|HAMAP-Rule:MF_01953}; OrderedLocusNames=HH_0408;
OS Helicobacter hepaticus (strain ATCC 51449 / 3B1).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=235279;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MU94-1;
RX PubMed=11500473; DOI=10.1128/iai.69.9.5914-5920.2001;
RA Beckwith C.S., McGee D.J., Mobley H.L.T., Riley L.K.;
RT "Cloning, expression, and catalytic activity of Helicobacter hepaticus
RT urease.";
RL Infect. Immun. 69:5914-5920(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51449 / 3B1;
RX PubMed=12810954; DOI=10.1073/pnas.1332093100;
RA Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M.,
RA Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R.,
RA Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B.,
RA Shen Z., Weber J., Frosch M., Fox J.G.;
RT "The complete genome sequence of the carcinogenic bacterium Helicobacter
RT hepaticus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003).
RN [3]
RP INDUCTION.
RX PubMed=16339943; DOI=10.1099/mic.0.28188-0;
RA Belzer C., Stoof J., Beckwith C.S., Kuipers E.J., Kusters J.G.,
RA van Vliet A.H.M.;
RT "Differential regulation of urease activity in Helicobacter hepaticus and
RT Helicobacter pylori.";
RL Microbiology 151:3989-3995(2005).
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_01953};
CC -!- COFACTOR:
CC Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01953};
CC Note=Binds 2 nickel ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01953};
CC -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC urea (urease route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01953}.
CC -!- SUBUNIT: Heterohexamer of 3 UreA (alpha) and 3 UreB (beta) subunits.
CC {ECO:0000255|HAMAP-Rule:MF_01953}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01953}.
CC -!- INDUCTION: By nickel ions. {ECO:0000269|PubMed:16339943}.
CC -!- PTM: Carboxylation allows a single lysine to coordinate two nickel
CC ions. {ECO:0000255|HAMAP-Rule:MF_01953}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Urease alpha subunit family. {ECO:0000255|HAMAP-Rule:MF_01953}.
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; AF332656; AAK69199.1; -; Genomic_DNA.
DR EMBL; AE017125; AAP77005.1; -; Genomic_DNA.
DR RefSeq; WP_011115250.1; NC_004917.1.
DR AlphaFoldDB; Q93PJ4; -.
DR SMR; Q93PJ4; -.
DR STRING; 235279.HH_0408; -.
DR MEROPS; M38.982; -.
DR EnsemblBacteria; AAP77005; AAP77005; HH_0408.
DR KEGG; hhe:HH_0408; -.
DR eggNOG; COG0804; Bacteria.
DR HOGENOM; CLU_000980_0_0_7; -.
DR OMA; GFDSHIH; -.
DR OrthoDB; 157757at2; -.
DR BRENDA; 3.5.1.5; 7587.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000002495; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009039; F:urease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00375; Urease_alpha; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR HAMAP; MF_01953; Urease_alpha; 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; IPR017950; Urease_AS.
DR InterPro; IPR005848; Urease_asu.
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 PRINTS; PR01752; UREASE.
DR SUPFAM; SSF51338; SSF51338; 2.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01792; urease_alph; 1.
DR PROSITE; PS01120; UREASE_1; 1.
DR PROSITE; PS00145; UREASE_2; 1.
DR PROSITE; PS51368; UREASE_3; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Metal-binding; Nickel; Reference proteome.
FT CHAIN 1..569
FT /note="Urease subunit beta"
FT /id="PRO_0000234158"
FT DOMAIN 131..569
FT /note="Urease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT ACT_SITE 322
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 136
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 138
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
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|HAMAP-Rule:MF_01953"
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|HAMAP-Rule:MF_01953"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 248
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 274
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 362
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT MOD_RES 219
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
SQ SEQUENCE 569 AA; 61510 MW; 2825D1E6406F6429 CRC64;
MIKISRKQYA SMYGPTTGDK VRLGDTNLFA EIEKDYTLYG EEIKFGGGKT IRDGMAQSAS
TYTNELDAVI TNAMIIDYTG IYKADIGIKG GKIVGIGKAG NPDTQDSVNE AMVVGAATEV
IAGEGQIITA GGIDTHIHFI SPTQIPTALY SGVTTMIGGG TGPAAGTNAT TCTPGKWNMH
QMLRAAESYA MNLGFFGKGN SSNEEGLEEQ IKAGALGLKV HEDWGSTPAA INHALNVAQK
YDVQVAIHTD TLNEAGCVED TMKAIDGRTI HTFHTEGAGG GHAPDIIKAA GEPNILPAST
NPTIPFTKNT ADEHLDMLMV CHHLDKKIKE DVAFADSRIR PETIAAEDTL HDMGIFSITS
SDSQAMGRVG EVITRTWQTA DKCKNEFGAL KEECGENDNF RIKRYISKYT INPAIAHGIS
EYVGSVEVGK FADLVLWKPS MFGIKPEMIL KNGMIVAAKI GDSNASIPTP EPVVYAPMFG
SYGKAKYNCA ITFVSKIAYD CHIKEELGLE RILLPVKNCR NITKKDMKFN DVITPIEVNP
ETYEVRVNNT KITSKPVEKV SLGQLYCLF
