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URE1_YEREN
ID   URE1_YEREN              Reviewed;         572 AA.
AC   P31494;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 3.
DT   03-AUG-2022, entry version 121.
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}; Synonyms=yeuC;
OS   Yersinia enterocolitica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=6471/76 / Serotype O:3;
RX   PubMed=8500886; DOI=10.1128/iai.61.6.2498-2504.1993;
RA   Skurnik M., Batsford S., Mertz A.K.H., Schiltz E., Toivanen P.;
RT   "The putative arthritogenic cationic 19-kilodalton antigen of Yersinia
RT   enterocolitica is a urease beta-subunit.";
RL   Infect. Immun. 61:2498-2504(1993).
RN   [2]
RP   ROLE IN VIRULENCE.
RC   STRAIN=W22703 / Serogroup O:9;
RX   PubMed=7558281; DOI=10.1128/iai.63.10.3790-3795.1995;
RA   de Koning-Ward T.F., Robins-Browne R.M.;
RT   "Contribution of urease to acid tolerance in Yersinia enterocolitica.";
RL   Infect. Immun. 63:3790-3795(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A2635 / Serotype O:8;
RX   PubMed=8045421; DOI=10.1016/0378-1119(94)90318-2;
RA   de Koning-Ward T.F., Ward A.C., Robins-Browne R.M.;
RT   "Characterisation of the urease-encoding gene complex of Yersinia
RT   enterocolitica.";
RL   Gene 145:25-32(1994).
CC   -!- FUNCTION: Expression of the urease operon increases the likelihood of
CC       bacterial survival by contibuting to acid resistance in vitro and in
CC       vivo in BALB/c mice. Y.enterocolitica enters the body via an oral path
CC       and must survive the acidic stomach before being able to colonize the
CC       intestinal mucosa (PubMed:7558281). {ECO:0000269|PubMed:7558281}.
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}.
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DR   EMBL; Z18865; CAA79316.1; -; Genomic_DNA.
DR   EMBL; L24101; AAA50996.1; -; Genomic_DNA.
DR   PIR; S36028; S36028.
DR   RefSeq; WP_011815716.1; NZ_NWMR01000089.1.
DR   AlphaFoldDB; P31494; -.
DR   SMR; P31494; -.
DR   MEROPS; M38.982; -.
DR   PATRIC; fig|630.32.peg.1788; -.
DR   UniPathway; UPA00258; UER00370.
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   Cytoplasm; Hydrolase; Metal-binding; Nickel; Virulence.
FT   CHAIN           1..572
FT                   /note="Urease subunit alpha"
FT                   /id="PRO_0000067565"
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"
FT   CONFLICT        30..31
FT                   /note="IE -> MQ (in Ref. 1; CAA79316)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        67
FT                   /note="V -> GY (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        69..83
FT                   /note="DLVITNVTIVDARLG -> EFSHNQRHYCCSPFR (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        97
FT                   /note="A -> V (in Ref. 1; CAA79316)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        115
FT                   /note="M -> L (in Ref. 1; CAA79316)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        138
FT                   /note="S -> T (in Ref. 1; CAA79316)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        406
FT                   /note="L -> V (in Ref. 1; CAA79316)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        441
FT                   /note="D -> V (in Ref. 1; CAA79316)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   572 AA;  61083 MW;  B9A36459DDC3E963 CRC64;
     MPQISRQEYA GLFGPTTGDK IRLGDTNLFI EIEKDLRGYG EESVYGGGKS LRDGMGANNH
     LTRDNGVLDL VITNVTIVDA RLGVIKADVG IRDGKIAGIG KSGNPGVMDG VTPGMVVGVS
     TDAISGEHLI LTAAGIDSHI HLISPQQAYH ALSNGVATFF GGGIGPTDGT NGTTVTPGPW
     NIRQMLRSVE GLPVNVGILG KGNSYGRGPL LEQAIAGVVG YKVHEDWGAT ANALRHSLRM
     ADEMDIQVSV HTDSLNECGY VEDTIDAFEG RTIHTFHTEG AGGGHAPDII RVASQPNVLP
     SSTNPTLPYG VNSQAELFDM IMVCHNLNPN VPADVSFAES RVRPETIAAE NVLHDMGVIS
     MFSSDSQAMG RVGENWLRVM QTANAMKASR GKLPEDAPGN DNFRVLRYVA KITINPAIAQ
     GVSHVIGSVE VGKMADLVLW DPRFFGAKPK MVIKGGMINW AAMGDPNASL PTPQPVFYRP
     MFGAMGKTMQ DTCVTFVSQA ALDDGVKEKA GLDRQVIAVK NCRTISKHDL VRNDQTPNIE
     VDPETFAVKV DGVHATCEPI DTAAMNQRYF FG
 
 
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