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Database: UniProt
Entry: J2K5M1_9ACTN
LinkDB: J2K5M1_9ACTN
Original site: J2K5M1_9ACTN 
ID   J2K5M1_9ACTN            Unreviewed;       568 AA.
AC   J2K5M1;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   16-OCT-2019, entry version 54.
DE   RecName: Full=Urease subunit alpha {ECO:0000256|HAMAP-Rule:MF_01953};
DE            EC=3.5.1.5 {ECO:0000256|HAMAP-Rule:MF_01953};
DE   AltName: Full=Urea amidohydrolase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01953};
GN   Name=ureC {ECO:0000256|HAMAP-Rule:MF_01953,
GN   ECO:0000313|EMBL:EJJ07790.1};
GN   ORFNames=SU9_06690 {ECO:0000313|EMBL:EJJ07790.1};
OS   Streptomyces auratus AGR0001.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1160718 {ECO:0000313|EMBL:EJJ07790.1, ECO:0000313|Proteomes:UP000009036};
RN   [1] {ECO:0000313|EMBL:EJJ07790.1, ECO:0000313|Proteomes:UP000009036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AGR0001 {ECO:0000313|EMBL:EJJ07790.1,
RC   ECO:0000313|Proteomes:UP000009036};
RX   PubMed=22965094; DOI=10.1128/JB.01155-12;
RA   Han X., Li M., Ding Z., Zhao J., Ji K., Wen M., Lu T.;
RT   "Genome Sequence of Streptomyces auratus Strain AGR0001, a
RT   Phoslactomycin-Producing Actinomycete.";
RL   J. Bacteriol. 194:5472-5473(2012).
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:0000256|HAMAP-Rule:MF_01953,
CC         ECO:0000256|SAAS:SAAS01119912};
CC   -!- COFACTOR:
CC       Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01953,
CC         ECO:0000256|PIRSR:PIRSR611612-51};
CC       Note=Binds 2 nickel ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01953, ECO:0000256|PIRSR:PIRSR611612-51};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3)
CC       from urea (urease route): step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01953, ECO:0000256|SAAS:SAAS00317636}.
CC   -!- SUBUNIT: May form a heterohexamer of 3 UreC (alpha) and 3 UreAB
CC       (gamma/beta) subunits. May also form a heterotrimer of UreA
CC       (gamma), UreB (beta) and UreC (alpha) subunits. Three
CC       heterotrimers associate to form the active enzyme.
CC       {ECO:0000256|HAMAP-Rule:MF_01953}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01953,
CC       ECO:0000256|PROSITE-ProRule:PRU00700,
CC       ECO:0000256|SAAS:SAAS00548017}.
CC   -!- PTM: Carbamylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000256|HAMAP-Rule:MF_01953,
CC       ECO:0000256|PIRSR:PIRSR611612-50}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. Urease alpha subunit family. {ECO:0000256|HAMAP-
CC       Rule:MF_01953, ECO:0000256|RuleBase:RU004158,
CC       ECO:0000256|SAAS:SAAS00849550}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EJJ07790.1}.
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DR   EMBL; AJGV01000052; EJJ07790.1; -; Genomic_DNA.
DR   STRING; 1160718.SU9_06690; -.
DR   EnsemblBacteria; EJJ07790; EJJ07790; SU9_06690.
DR   PATRIC; fig|1160718.3.peg.1361; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000009036; Unassembled WGS sequence.
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   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; 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   PROSITE; PS01120; UREASE_1; 1.
DR   PROSITE; PS51368; UREASE_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000009036};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01953, ECO:0000256|PROSITE-
KW   ProRule:PRU00700, ECO:0000256|SAAS:SAAS00317631};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01953, ECO:0000256|PROSITE-
KW   ProRule:PRU00700, ECO:0000256|SAAS:SAAS00321417,
KW   ECO:0000313|EMBL:EJJ07790.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01953,
KW   ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|SAAS:SAAS00321440};
KW   Nickel {ECO:0000256|HAMAP-Rule:MF_01953,
KW   ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|SAAS:SAAS00317628};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009036}.
FT   DOMAIN      129    568       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    317    317       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                52, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   METAL       134    134       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       136    136       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       214    214       Nickel 1; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       214    214       Nickel 2; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       243    243       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       269    269       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       357    357       Nickel 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                51}.
FT   BINDING     216    216       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     214    214       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01953, ECO:0000256|PIRSR:
FT                                PIRSR611612-50}.
SQ   SEQUENCE   568 AA;  59140 MW;  09A573EFCBD5B899 CRC64;
     MTIDPHEYAS VHGPRAGDRV VLGDSGLVVR VESDAQKPGD EFLAGFGKTA RDGLHLKAAA
     VRETCDVVIS NVLVIDAVQG IRKVSIGIRE GRIHAIGRAG NPDTLDGVDV VVGTGTSIVS
     GEGMIATAGA VDTHVHLLSP RVMEASLASG VTTIIGQEFG PVWGVGVNSP WALGHAFKAF
     DAWPVNIGFL GRGSSSGEAP LVEALAEGGA CGFKVHEDMG AHARALDTAL RVAEDHDVQV
     ALHSDGLNEC LTVEDTLRVL DGRTIHAFHI EGCGGGHVPN VLKMAGVPNV IGSSTNPTLP
     FGRDAVAEHY GMIVSVHDLK TDLPGDAAMA RDRIRAGTMG AEDVLHDLGA IGITSSDAQG
     MGRAGETVRR TFAMAGKMKA ELGPLLPRNG EAGDGPHDDN ARVLRYVAKL TINPALAHGL
     SHEIGSIEVG KMADIVLWKP QFFGAKPQLV LKSGFPAYGV TGDPNAATDT CEPLVLGPQF
     GAYGATPAEI SVAFVARAAA EQGGDSMPTR RRRVAVRGTR GIGPGDLVHN SRIGQVQVDG
     RSGLVTLDGA LMRSEPADSV SLPRLYFL
//
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