URE1_HELFC
ID URE1_HELFC Reviewed; 569 AA.
AC Q08716; E7A955; Q9R3B3;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 140.
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};
GN OrderedLocusNames=Hfelis_11980;
OS Helicobacter felis (strain ATCC 49179 / NCTC 12436 / CS1).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=936155;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 49179 / NCTC 12436 / CS1;
RX PubMed=8412683; DOI=10.1111/j.1365-2958.1993.tb01693.x;
RA Ferrero R.L., Labigne A.;
RT "Cloning, expression and sequencing of Helicobacter felis urease genes.";
RL Mol. Microbiol. 9:323-333(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49179 / NCTC 12436 / CS1;
RA Arnold A., Zigova Z., Lawley T., Falkow S., Bentley S., Aslett M.,
RA Muller A.;
RT "Comparative whole genome analysis of the carcinogenic bacterial pathogen
RT Helicobacter felis.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=ATCC 49179 / NCTC 12436 / CS1;
RX PubMed=1452359; DOI=10.1128/iai.60.12.5259-5266.1992;
RA Turbett G.R., Hoej P.B., Horne R., Mee B.J.;
RT "Purification and characterization of the urease enzymes of Helicobacter
RT species from humans and animals.";
RL Infect. Immun. 60:5259-5266(1992).
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 -!- 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; X69080; CAA48826.1; -; Genomic_DNA.
DR EMBL; FQ670179; CBY83282.1; -; Genomic_DNA.
DR PIR; C49215; C49215.
DR PIR; S35291; S35291.
DR RefSeq; WP_013469646.1; NC_014810.2.
DR AlphaFoldDB; Q08716; -.
DR SMR; Q08716; -.
DR STRING; 936155.HFELIS_11980; -.
DR MEROPS; M38.982; -.
DR EnsemblBacteria; CBY83282; CBY83282; HFELIS_11980.
DR GeneID; 36133721; -.
DR KEGG; hfe:HFELIS_11980; -.
DR eggNOG; COG0804; Bacteria.
DR HOGENOM; CLU_000980_0_0_7; -.
DR OMA; GFDSHIH; -.
DR OrthoDB; 157757at2; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000007934; 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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Metal-binding; Nickel.
FT CHAIN 1..569
FT /note="Urease subunit beta"
FT /id="PRO_0000067530"
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"
FT CONFLICT 414
FT /note="A -> G (in Ref. 1; CAA48826)"
FT /evidence="ECO:0000305"
FT CONFLICT 512..514
FT /note="VVL -> AAP (in Ref. 1; CAA48826)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 569 AA; 61789 MW; 1DDE48C916EF0ED0 CRC64;
MKKISRKEYV SMYGPTTGDR VRLGDTDLIL EVEHDCTTYG EEIKFGGGKT IRDGMSQTNS
PSSYELDLVL TNALIVDYTG IYKADIGIKD GKIAGIGKAG NKDMQDGVDN NLCVGPATEA
LAAEGLIVTA GGIDTHIHFI SPQQIPTAFA SGVTTMIGGG TGPADGTNAT TITPGRANLK
SMLRAAEEYA MNLGFLAKGN VSYEPSLRDQ IEAGAIGFKI HEDWGSTPAA IHHCLNVADE
YDVQVAIHTD TLNEAGCVED TLEAIAGRTI HTFHTEGAGG GHAPDVIKMA GEFNILPAST
NPTIPFTKNT EAEHMDMLMV CHHLDKSIKE DVQFADSRIR PQTIAAEDQL HDMGIFSITS
SDSQAMGRVG EVITRTWQTA DKNKKEFGRL KEEKGDNDNF RIKRYISKYT INPAIAHGIS
DYVGSVEVGK YADLVLWSPA FFGIKPNMII KGGFIALSQM GDANASIPTP QPVYYREMFG
HHGKNKFDTN ITFVSQAAYK AGIKEELGLD RVVLPVKNCR NITKKDLKFN DVTAHIDVNP
ETYKVKVDGK EVTSKAADEL SLAQLYNLF
