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Database: UniProt
Entry: URE1_ECO57
LinkDB: URE1_ECO57
Original site: URE1_ECO57 
ID   URE1_ECO57              Reviewed;         568 AA.
AC   Q8XAG0; Q7AFH5;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   16-OCT-2019, entry version 114.
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=ureC1 {ECO:0000255|HAMAP-Rule:MF_01953};
GN   OrderedLocusNames=Z1145, ECs1324;
GN   and
GN   Name=ureC2 {ECO:0000255|HAMAP-Rule:MF_01953}; OrderedLocusNames=Z1584;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
RN   [3]
RP   ABSENCE OF UREASE.
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=15470125; DOI=10.1099/mic.0.27280-0;
RA   Nakano M., Iida T., Honda T.;
RT   "Urease activity of enterohaemorrhagic Escherichia coli depends on a
RT   specific one-base substitution in ureD.";
RL   Microbiology 150:3483-3489(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+);
CC         Xref=Rhea:RHEA:20557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16199, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938;
CC         EC=3.5.1.5; 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)
CC       from urea (urease route): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01953}.
CC   -!- SUBUNIT: Heterotrimer of UreA (gamma), UreB (beta) and UreC
CC       (alpha) subunits. Three heterotrimers associate to form the active
CC       enzyme. {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
CC       superfamily. Urease alpha subunit family. {ECO:0000255|HAMAP-
CC       Rule:MF_01953}.
CC   -!- CAUTION: Neither O157 strain expresses urease due to a truncation
CC       of ureD, the last gene of the probable operon. Urease activity is
CC       restored in O157 / Sakai upon complementation with wild-type ureD.
CC       {ECO:0000305}.
CC   -!- CAUTION: This region of the chromosome is duplicated in strain
CC       O157:H7 / EDL933 but not in O157:H7 / Sakai. {ECO:0000305}.
DR   EMBL; AE005174; AAG55290.1; -; Genomic_DNA.
DR   EMBL; AE005174; AAG55699.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34747.1; -; Genomic_DNA.
DR   PIR; D90794; D90794.
DR   PIR; G85654; G85654.
DR   RefSeq; NP_309351.1; NC_002695.1.
DR   RefSeq; WP_001301487.1; NZ_LPWC02000004.1.
DR   SMR; Q8XAG0; -.
DR   STRING; 155864.EDL933_1505; -.
DR   MEROPS; M38.982; -.
DR   PRIDE; Q8XAG0; -.
DR   EnsemblBacteria; AAG55290; AAG55290; Z1145.
DR   EnsemblBacteria; AAG55699; AAG55699; Z1584.
DR   EnsemblBacteria; BAB34747; BAB34747; BAB34747.
DR   GeneID; 913507; -.
DR   KEGG; ece:Z1145; -.
DR   KEGG; ece:Z1584; -.
DR   KEGG; ecs:ECs1324; -.
DR   PATRIC; fig|386585.9.peg.1429; -.
DR   eggNOG; ENOG4105CQM; Bacteria.
DR   eggNOG; COG0804; LUCA.
DR   HOGENOM; HOG000075064; -.
DR   KO; K01428; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Nickel;
KW   Reference proteome.
FT   CHAIN         1    568       Urease subunit alpha.
FT                                /FTId=PRO_0000234155.
FT   DOMAIN      130    568       Urease. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   ACT_SITE    321    321       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   METAL       135    135       Nickel 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       137    137       Nickel 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       218    218       Nickel 1; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       218    218       Nickel 2; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       247    247       Nickel 2; via pros nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       273    273       Nickel 2; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       361    361       Nickel 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   BINDING     220    220       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   MOD_RES     218    218       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
SQ   SEQUENCE   568 AA;  60626 MW;  AC39B7B701481361 CRC64;
     MMSNISRQAY ADMFGPTTGD KIRLADTELW IEVEDDLTTY GEEVKFGGGK VIRDGMGQGQ
     MLSAGCADLV LTNALIIDYW GIVKADIGVK DGRIFAIGKA GNPDIQPNVT IPIGVSTEII
     AAEGRIVTAG GVDTHIHWIC PQQAEEALTS GITTMIGGGT GPTAGSNATT CTPGPWYIYQ
     MLQAADSLPV NIGLLGKGNC SNPDALREQV AAGVIGLKIH EDWGATPAVI NCALTVADEM
     DVQVALHSDT LNESGFVEDT LTAIGGRTIH TFHTEGAGGG HAPDIITACA HPNILPSSTN
     PTLPYTVNTI DEHLDMLMVC HHLDPDIAED VAFAESRIRQ ETIAAEDVLH DLGAFSLTSS
     DSQAMGRVGE VVLRTWQVAH RMKVQRGPLP EESGDNDNVR VKRYIAKYTI NPALTHGIAH
     EVGSIEVGKL ADLVLWSPAF FGVKPATIVK GGMIAMAPMG DINGSIPTPQ PVHYRPMFAA
     LGSARHRCRV TFLSQAAAAN GVAEQLNLHS TTAVVKGCRT VQKADMRHNS LLPDITVDSQ
     TYEVRINGEL ITSEPADILP MAQRYFLF
//
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