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Database: UniProt
Entry: URE1_STAS1
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ID   URE1_STAS1              Reviewed;         571 AA.
AC   Q4A0J5;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-OCT-2019, entry version 103.
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=SSP0263;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 /
OS   DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K.,
RA   Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S.,
RA   Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-6, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=8042901; DOI=10.1007/bf00288948;
RA   Schaefer U.K., Kaltwasser H.;
RT   "Urease from Staphylococcus saprophyticus: purification,
RT   characterization and comparison to Staphylococcus xylosus urease.";
RL   Arch. Microbiol. 161:393-399(1994).
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         ECO:0000269|PubMed:8042901};
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=9.5 mM for urea (at 37 degrees Celsius and pH 7.0)
CC         {ECO:0000269|PubMed:8042901};
CC         Vmax=1.979 mmol/min/mg enzyme {ECO:0000269|PubMed:8042901};
CC       pH dependence:
CC         Optimum pH is 7.0 in phosphate buffer.
CC         {ECO:0000269|PubMed:8042901};
CC       Temperature dependence:
CC         Optimum temperature is 55 degrees Celsius.
CC         {ECO:0000269|PubMed:8042901};
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}.
DR   EMBL; AP008934; BAE17408.1; -; Genomic_DNA.
DR   RefSeq; WP_002482218.1; NZ_MTGA01000037.1.
DR   SMR; Q4A0J5; -.
DR   STRING; 342451.SSP0263; -.
DR   EnsemblBacteria; BAE17408; BAE17408; SSP0263.
DR   GeneID; 3616069; -.
DR   KEGG; ssp:SSP0263; -.
DR   eggNOG; ENOG4105CQM; Bacteria.
DR   eggNOG; COG0804; LUCA.
DR   HOGENOM; HOG000075064; -.
DR   KO; K01428; -.
DR   OMA; GFDSHIH; -.
DR   OrthoDB; 157757at2; -.
DR   BioCyc; SSAP342451:G1G2H-256-MONOMER; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000006371; 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   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase;
KW   Metal-binding; Nickel; Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:8042901}.
FT   CHAIN         2    571       Urease subunit alpha.
FT                                /FTId=PRO_0000234182.
FT   DOMAIN      133    571       Urease. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   ACT_SITE    324    324       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   METAL       138    138       Nickel 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       140    140       Nickel 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       221    221       Nickel 1; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       221    221       Nickel 2; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       250    250       Nickel 2; via pros nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       276    276       Nickel 2; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01953}.
FT   METAL       364    364       Nickel 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   BINDING     223    223       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
FT   MOD_RES     221    221       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01953}.
SQ   SEQUENCE   571 AA;  61942 MW;  199052E53293A937 CRC64;
     MSFKMTQSQY TSLYGPTVGD SVRLGDTNLF ARVERDYATY GDEAAFGGGK SIRDGMAQNP
     NVTRDDKQVA DLVITNAMII DYDKIVKADI GVKNGYIMKI GKAGNPDIMD NVDIIIGATT
     DIISAEGKIV TAGGIDTHVH FINPEQSQVA LESGITTHIG GGTGASEGTK ATTVTPGPWH
     LHRMLLAAES LPLNIGFTGK GQAVNHTALV EQIHAGAIGL KVHEDWGATP SALDHALQVA
     DDYDVQIALH ADTLNEAGFM EETMAAVKDR VLHMYHTEGA GGGHAPDLIK SAAYANILPS
     STNPTLPYTV NTIDEHLDMV MITHHLNASI PEDIAFADSR IRKETIAAED VLQDMGVFSM
     VSSDSQAMGR VGEVITRTWQ VAHRMKEQRG LLDGDSEYND NNRIKRYIAK YTINPAITHG
     ISDYVGSIDE GKLADIILWE PAFFGVKPDV IVKGGLINAA INGDANGSIP TSEPLKYRKM
     YGQLGGNLQS TSMTFVSTTA YENDIGKLLG LKRKLRPVHN IRKLSKKDMK NNNATPDLDV
     DPQTYEVFVD GEKITSEPAT ELPLTQRYFL F
//
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