URE1_YERPE
ID URE1_YERPE Reviewed; 572 AA.
AC Q9ZFR9; Q0WDM2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 159.
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};
GN OrderedLocusNames=YPO2667, y1239, YP_2468;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND LACK OF ROLE IN VIRULENCE.
RC STRAIN=6/69M;
RX PubMed=11119503; DOI=10.1128/iai.69.1.170-176.2001;
RA Sebbane F., Devalckenaere A., Foulon J., Carniel E., Simonet M.;
RT "Silencing and reactivation of urease in Yersinia pestis is determined by
RT one G residue at a specific position in the ureD gene.";
RL Infect. Immun. 69:170-176(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
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}.
CC -!- CAUTION: The last gene of this probable operon, ureD, gives rise to a
CC truncated protein. Absence of ureD prevents expression of active
CC urease. Correction of the mutation does not effect virulence in mice in
CC any detectable fashion, suggesting urease is not important in the
CC virulence of Y.pestis (PubMed:11119503). {ECO:0000305|PubMed:11119503}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM84814.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF095636; AAC78634.1; -; Genomic_DNA.
DR EMBL; AL590842; CAL21286.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM84814.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE017042; AAS62668.1; -; Genomic_DNA.
DR PIR; AC0325; AC0325.
DR RefSeq; WP_002212229.1; NZ_WUCM01000006.1.
DR RefSeq; YP_002347616.1; NC_003143.1.
DR AlphaFoldDB; Q9ZFR9; -.
DR SMR; Q9ZFR9; -.
DR IntAct; Q9ZFR9; 5.
DR STRING; 214092.YPO2667; -.
DR MEROPS; M38.982; -.
DR PaxDb; Q9ZFR9; -.
DR EnsemblBacteria; AAM84814; AAM84814; y1239.
DR EnsemblBacteria; AAS62668; AAS62668; YP_2468.
DR GeneID; 66844634; -.
DR KEGG; ype:YPO2667; -.
DR KEGG; ypk:y1239; -.
DR KEGG; ypm:YP_2468; -.
DR PATRIC; fig|214092.21.peg.3101; -.
DR eggNOG; COG0804; Bacteria.
DR HOGENOM; CLU_000980_2_0_6; -.
DR OMA; CHHLSHD; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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; 1.
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; Reference proteome.
FT CHAIN 1..572
FT /note="Urease subunit alpha"
FT /id="PRO_0000067566"
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"
SQ SEQUENCE 572 AA; 61019 MW; F3D9D3223E660AAF CRC64;
MPQISRQEYA GLFGPTTGDK IRLGDTNLFI EIEKDLRGYG EESVYGGGKS LRDGMGANNN
LTRDNGVLDL VITNVTIVDA RLGVIKADVG IRDGKIAGIG KSGNPGVMDG VTQGMVVGVS
TDAISGEHLI LTAAGIDSHI HLISPQQAYH ALSNGVATFF GGGIGPTDGT NGTTVTPGPW
NIRQMLRSIE GLPVNVGILG KGNSYGRGPL LEQAIAGVVG YKVHEDWGAT ANALRHALRM
ADEVDIQVSV HTDSLNECGY VEDTIDAFEG RTIHTFHTEG AGGGHAPDII RVASQTNVLP
SSTNPTLPYG VNSQAELFDM IMVCHNLNPN VPADVSFAES RVRPETIAAE NVLHDMGVIS
MFSSDSQAMG RVGENWLRIL QTADAMKAAR GKLPEDAAGN DNFRVLRYVA KITINPAITQ
GVSHVIGSVE VGKMADLVLW DPRFFGAKPK MVIKGGMINW AAMGDPNASL PTPQPVFYRP
MFGAMGKTLQ DTCVTFVSQA ALDDGVKEKA GLDRQVIAVK NCRTISKRDL VRNDQTPNIE
VDPETFAVKV DGVHATCEPI ATASMNQRYF FG
