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Database: UniProt
Entry: A0A0K2X2I9_9HELI
LinkDB: A0A0K2X2I9_9HELI
Original site: A0A0K2X2I9_9HELI 
ID   A0A0K2X2I9_9HELI        Unreviewed;       569 AA.
AC   A0A0K2X2I9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   13-NOV-2019, entry version 28.
DE   RecName: Full=Urease subunit beta {ECO:0000256|HAMAP-Rule:MF_01953};
DE            EC=3.5.1.5 {ECO:0000256|HAMAP-Rule:MF_01953};
DE   AltName: Full=Urea amidohydrolase subunit beta {ECO:0000256|HAMAP-Rule:MF_01953};
GN   Name=ureB {ECO:0000256|HAMAP-Rule:MF_01953};
GN   ORFNames=HAL011_03270 {ECO:0000313|EMBL:CRF40565.1}, HAL013_08960
GN   {ECO:0000313|EMBL:CRF42699.1}, HAL09_03620
GN   {ECO:0000313|EMBL:CRF43809.1};
OS   Helicobacter ailurogastricus.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1578720 {ECO:0000313|EMBL:CRF40565.1, ECO:0000313|Proteomes:UP000038622};
RN   [1] {ECO:0000313|EMBL:CRF40565.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ASB11 {ECO:0000313|EMBL:CRF40565.1}, ASB13
RC   {ECO:0000313|EMBL:CRF42699.1}, and ASB9 {ECO:0000313|EMBL:CRF43809.1};
RA   Misic A.M., Cain C., Morris D.O., Rankin S., Beiting D.;
RT   "Whole genome sequences of four Staphylococcus schleiferi canine
RT   isolates.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000038622, ECO:0000313|Proteomes:UP000041394, ECO:0000313|Proteomes:UP000045175}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jaenicke S.;
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU000510, 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         ECO:0000256|RuleBase:RU000510};
CC       Note=Binds 2 nickel ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01953, ECO:0000256|PIRSR:PIRSR611612-51,
CC       ECO:0000256|RuleBase:RU000510};
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: Heterohexamer of 3 UreA (alpha) and 3 UreB (beta)
CC       subunits. {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|PIRSR:PIRSR611612-50}.
CC   -!- PTM: Carboxylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000256|HAMAP-Rule:MF_01953}.
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 orthologous protein is known as the alpha subunit
CC       (UreC) in most other bacteria. {ECO:0000256|HAMAP-Rule:MF_01953}.
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DR   EMBL; CDML01000010; CRF40565.1; -; Genomic_DNA.
DR   EMBL; CDMH01000039; CRF42699.1; -; Genomic_DNA.
DR   EMBL; CDMN01000012; CRF43809.1; -; Genomic_DNA.
DR   RefSeq; WP_053941315.1; NZ_FZMH01000037.1.
DR   EnsemblBacteria; CRF40565; CRF40565; HAL011_03270.
DR   EnsemblBacteria; CRF42699; CRF42699; HAL013_08960.
DR   EnsemblBacteria; CRF43809; CRF43809; HAL09_03620.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000038622; Unassembled WGS sequence.
DR   Proteomes; UP000041394; Unassembled WGS sequence.
DR   Proteomes; UP000045175; 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   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 {ECO:0000313|Proteomes:UP000038622,
KW   ECO:0000313|Proteomes:UP000041394, ECO:0000313|Proteomes:UP000045175};
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|RuleBase:RU000510,
KW   ECO:0000256|SAAS:SAAS00321417};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01953,
KW   ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|RuleBase:RU000510,
KW   ECO:0000256|SAAS:SAAS00321440};
KW   Nickel {ECO:0000256|HAMAP-Rule:MF_01953,
KW   ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|RuleBase:RU000510,
KW   ECO:0000256|SAAS:SAAS00317628}.
FT   DOMAIN      131    569       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    322    322       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                52, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   METAL       136    136       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       138    138       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       219    219       Nickel 1; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       219    219       Nickel 2; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       248    248       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       274    274       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       362    362       Nickel 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                51}.
FT   BINDING     221    221       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     219    219       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01953, ECO:0000256|PIRSR:
FT                                PIRSR611612-50}.
SQ   SEQUENCE   569 AA;  61978 MW;  B06077B04B45CA85 CRC64;
     MKKISRKEYV SMYGPTTGDK VRLGDTDLIL EVEHDCTTYG EEIKFGGGKT IRDGMGQTNS
     PSSHELDLVI TNALIVDYTG IYKADIGIKN GKIHGIGKAG NKDLQDGVCN RLCVGPATEA
     LAGEGLIVTA GGIDTHIHFI SPQQIPTAFA SGITTMIGGG TGPADGTNAT TITPGRWNLK
     EMLRASEEYA MNLGYLGKGN VSYEPSLTDQ LYAGAIGFKI HEDWGSTPSA INHALNIADK
     YDVQVAIHTD TLNEAGCVED TLQAIAGRTI HTFHTEGAGG GHAPDVIKMA GEFNILPAST
     NPTIPFTKNT EAEHMDMLMV CHHLDKNIKE DVEFADSRIR PQTIAAEDKL HDMGIFSITS
     SDSQAMGRVG EVITRTWQTA DKNKKEFGRL PEEKGDNDNF RIKRYIAKYT INPAIAHGIS
     EYVGSVEVGK YADLVLWSPA FFGIKPNMII KGGFIALSQM GDANASIPTP QPVYYREMFG
     HHGKAKFDTN ITFVSQVAYE NGIKEELGLQ RIVLPVKNCR NITKKDLKFN DVTAHIEVNP
     ETYKVKVDGN EVTSHAADKL PLAQLYNLF
//
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