URE1_YEREN
ID URE1_YEREN Reviewed; 572 AA.
AC P31494;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Urease subunit alpha {ECO:0000255|HAMAP-Rule:MF_01953};
DE EC=3.5.1.5 {ECO:0000255|HAMAP-Rule:MF_01953};
DE AltName: Full=Urea amidohydrolase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01953};
GN Name=ureC {ECO:0000255|HAMAP-Rule:MF_01953}; Synonyms=yeuC;
OS Yersinia enterocolitica.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=630;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=6471/76 / Serotype O:3;
RX PubMed=8500886; DOI=10.1128/iai.61.6.2498-2504.1993;
RA Skurnik M., Batsford S., Mertz A.K.H., Schiltz E., Toivanen P.;
RT "The putative arthritogenic cationic 19-kilodalton antigen of Yersinia
RT enterocolitica is a urease beta-subunit.";
RL Infect. Immun. 61:2498-2504(1993).
RN [2]
RP ROLE IN VIRULENCE.
RC STRAIN=W22703 / Serogroup O:9;
RX PubMed=7558281; DOI=10.1128/iai.63.10.3790-3795.1995;
RA de Koning-Ward T.F., Robins-Browne R.M.;
RT "Contribution of urease to acid tolerance in Yersinia enterocolitica.";
RL Infect. Immun. 63:3790-3795(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A2635 / Serotype O:8;
RX PubMed=8045421; DOI=10.1016/0378-1119(94)90318-2;
RA de Koning-Ward T.F., Ward A.C., Robins-Browne R.M.;
RT "Characterisation of the urease-encoding gene complex of Yersinia
RT enterocolitica.";
RL Gene 145:25-32(1994).
CC -!- FUNCTION: Expression of the urease operon increases the likelihood of
CC bacterial survival by contibuting to acid resistance in vitro and in
CC vivo in BALB/c mice. Y.enterocolitica enters the body via an oral path
CC and must survive the acidic stomach before being able to colonize the
CC intestinal mucosa (PubMed:7558281). {ECO:0000269|PubMed:7558281}.
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: 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_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}.
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DR EMBL; Z18865; CAA79316.1; -; Genomic_DNA.
DR EMBL; L24101; AAA50996.1; -; Genomic_DNA.
DR PIR; S36028; S36028.
DR RefSeq; WP_011815716.1; NZ_NWMR01000089.1.
DR AlphaFoldDB; P31494; -.
DR SMR; P31494; -.
DR MEROPS; M38.982; -.
DR PATRIC; fig|630.32.peg.1788; -.
DR UniPathway; UPA00258; UER00370.
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 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Metal-binding; Nickel; Virulence.
FT CHAIN 1..572
FT /note="Urease subunit alpha"
FT /id="PRO_0000067565"
FT DOMAIN 134..572
FT /note="Urease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT ACT_SITE 325
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 139
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 141
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 222
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 222
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 224
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 251
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 277
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 365
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 222
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT CONFLICT 30..31
FT /note="IE -> MQ (in Ref. 1; CAA79316)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="V -> GY (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 69..83
FT /note="DLVITNVTIVDARLG -> EFSHNQRHYCCSPFR (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="A -> V (in Ref. 1; CAA79316)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="M -> L (in Ref. 1; CAA79316)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="S -> T (in Ref. 1; CAA79316)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="L -> V (in Ref. 1; CAA79316)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="D -> V (in Ref. 1; CAA79316)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 572 AA; 61083 MW; B9A36459DDC3E963 CRC64;
MPQISRQEYA GLFGPTTGDK IRLGDTNLFI EIEKDLRGYG EESVYGGGKS LRDGMGANNH
LTRDNGVLDL VITNVTIVDA RLGVIKADVG IRDGKIAGIG KSGNPGVMDG VTPGMVVGVS
TDAISGEHLI LTAAGIDSHI HLISPQQAYH ALSNGVATFF GGGIGPTDGT NGTTVTPGPW
NIRQMLRSVE GLPVNVGILG KGNSYGRGPL LEQAIAGVVG YKVHEDWGAT ANALRHSLRM
ADEMDIQVSV HTDSLNECGY VEDTIDAFEG RTIHTFHTEG AGGGHAPDII RVASQPNVLP
SSTNPTLPYG VNSQAELFDM IMVCHNLNPN VPADVSFAES RVRPETIAAE NVLHDMGVIS
MFSSDSQAMG RVGENWLRVM QTANAMKASR GKLPEDAPGN DNFRVLRYVA KITINPAIAQ
GVSHVIGSVE VGKMADLVLW DPRFFGAKPK MVIKGGMINW AAMGDPNASL PTPQPVFYRP
MFGAMGKTMQ DTCVTFVSQA ALDDGVKEKA GLDRQVIAVK NCRTISKHDL VRNDQTPNIE
VDPETFAVKV DGVHATCEPI DTAAMNQRYF FG