URE1_PROMH
ID URE1_PROMH Reviewed; 567 AA.
AC P17086; B4EXN5;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 155.
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}; OrderedLocusNames=PMI3685;
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2687233; DOI=10.1128/jb.171.12.6414-6422.1989;
RA Jones B.D., Mobley H.L.T.;
RT "Proteus mirabilis urease: nucleotide sequence determination and comparison
RT with jack bean urease.";
RL J. Bacteriol. 171:6414-6422(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320;
RX PubMed=18375554; DOI=10.1128/jb.01981-07;
RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA Parkhill J., Mobley H.L.T.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(2008).
RN [3]
RP UREASE AS A VIRULENCE FACTOR.
RX PubMed=2180821; DOI=10.1128/iai.58.4.1120-1123.1990;
RA Jones B.D., Lockatell C.V., Johnson D.E., Warren J.W., Mobley H.L.T.;
RT "Construction of a urease-negative mutant of Proteus mirabilis: analysis of
RT virulence in a mouse model of ascending urinary tract infection.";
RL Infect. Immun. 58:1120-1123(1990).
RN [4]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-312; CYS-319; HIS-320; HIS-321;
RP HIS-472; HIS-527 AND HIS-533.
RX PubMed=8500894; DOI=10.1128/iai.61.6.2570-2577.1993;
RA Sriwanthana B., Mobley H.L.T.;
RT "Proteus mirabilis urease: histidine 320 of UreC is essential for urea
RT hydrolysis and nickel ion binding within the native enzyme.";
RL Infect. Immun. 61:2570-2577(1993).
RN [5]
RP INDUCTION.
RX PubMed=7678244; DOI=10.1128/jb.175.2.465-473.1993;
RA Nicholson E.B., Concaugh E.A., Foxall P.A., Island M.D., Mobley H.L.T.;
RT "Proteus mirabilis urease: transcriptional regulation by UreR.";
RL J. Bacteriol. 175:465-473(1993).
RN [6]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF VAL-267; GLY-422; MET-489 AND
RP ASP-537.
RX PubMed=7559355; DOI=10.1128/jb.177.19.5653-5660.1995;
RA Island M.D., Mobley H.L.T.;
RT "Proteus mirabilis urease: operon fusion and linker insertion analysis of
RT ure gene organization, regulation, and function.";
RL J. Bacteriol. 177:5653-5660(1995).
RN [7]
RP INTERACTION WITH UREA AND URED.
RX PubMed=11157956; DOI=10.1128/jb.183.4.1423-1433.2001;
RA Heimer S.R., Mobley H.L.T.;
RT "Interaction of Proteus mirabilis urease apoenzyme and accessory proteins
RT identified with yeast two-hybrid technology.";
RL J. Bacteriol. 183:1423-1433(2001).
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 ECO:0000269|PubMed:7559355, ECO:0000269|PubMed:8500894};
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: Probable heterotrimer of UreA (gamma), UreB (beta) and UreC
CC (alpha) subunits. Three heterotrimers associate to form the active
CC enzyme. The trimeric urease interacts with an accessory complex
CC composed of UreD, UreF and UreG, which is required for the assembly of
CC the nickel containing metallocenter of UreC. The UreE protein may also
CC play a direct role in nickel transfer to the urease apoprotein.
CC {ECO:0000269|PubMed:11157956}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01953}.
CC -!- INDUCTION: By urea. {ECO:0000269|PubMed:7678244}.
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; M31834; AAA25669.1; -; Genomic_DNA.
DR EMBL; AM942759; CAR47185.1; -; Genomic_DNA.
DR PIR; D43719; D43719.
DR RefSeq; WP_004245262.1; NC_010554.1.
DR AlphaFoldDB; P17086; -.
DR SMR; P17086; -.
DR STRING; 529507.PMI3685; -.
DR MEROPS; M38.982; -.
DR EnsemblBacteria; CAR47185; CAR47185; PMI3685.
DR GeneID; 6801207; -.
DR KEGG; pmr:PMI3685; -.
DR eggNOG; COG0804; Bacteria.
DR HOGENOM; CLU_000980_0_0_6; -.
DR OMA; GFDSHIH; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000008319; 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 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Metal-binding; Nickel; Reference proteome; Virulence.
FT CHAIN 1..567
FT /note="Urease subunit alpha"
FT /id="PRO_0000067547"
FT DOMAIN 129..567
FT /note="Urease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT ACT_SITE 320
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT BINDING 134
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 136
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 217
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 217
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 219
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 246
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 272
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 360
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 217
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT MUTAGEN 267
FT /note="V->VRRRI: Abrogates activity."
FT /evidence="ECO:0000269|PubMed:7559355"
FT MUTAGEN 312
FT /note="H->L: Reduces activity 30-fold."
FT /evidence="ECO:0000269|PubMed:8500894"
FT MUTAGEN 319
FT /note="C->A: Abrogates activity."
FT /evidence="ECO:0000269|PubMed:8500894"
FT MUTAGEN 320
FT /note="H->L: Abrogates activity and reduces binding to
FT nickel ions."
FT /evidence="ECO:0000269|PubMed:8500894"
FT MUTAGEN 321
FT /note="H->L: Abrogates activity."
FT /evidence="ECO:0000269|PubMed:8500894"
FT MUTAGEN 422
FT /note="G->GSVDG: Abrogates activity."
FT /evidence="ECO:0000269|PubMed:7559355"
FT MUTAGEN 472
FT /note="H->L: Reduces activity 12-fold."
FT /evidence="ECO:0000269|PubMed:8500894"
FT MUTAGEN 489
FT /note="M->MRRRI: Abrogates activity."
FT /evidence="ECO:0000269|PubMed:7559355"
FT MUTAGEN 527
FT /note="H->L: Reduces activity 6-fold."
FT /evidence="ECO:0000269|PubMed:8500894"
FT MUTAGEN 533
FT /note="H->L: Reduces activity 300-fold."
FT /evidence="ECO:0000269|PubMed:8500894"
FT MUTAGEN 537
FT /note="D->DRRRI: Reduces activity 25-fold."
FT /evidence="ECO:0000269|PubMed:7559355"
FT CONFLICT 454
FT /note="A -> R (in Ref. 1; AAA25669)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 567 AA; 60927 MW; E7747728624EC549 CRC64;
MKTISRQAYA DMFGPTTGDR LRLADTELFL EIEKDFTTYG EEVKFGGGKV IRDGMGQSQV
VSAECVDVLI TNAIILDYWG IVKADIGIKD GRIVGIGKAG NPDVQPNVDI VIGPGTEVVA
GEGKIVTAGG IDTHIHFICP QQAQEGLVSG VTTFIGGGTG PVAGTNATTV TPGIWNMYRM
LEAVDELPIN VGLFGKGCVS QPEAIREQIT AGAIGLKIHE DWGATPMAIH NCLNVADEMD
VQVAIHSDTL NEGGFYEETV KAIAGRVIHV FHTEGAGGGH APDVIKSVGE PNILPASTNP
TMPYTINTVD EHLDMLMVCH HLDPSIPEDV AFAESRIRRE TIAAEDILHD MGAISVMSSD
SQAMGRVGEV ILRTWQCAHK MKLQRGTLAG DSADNDNNRI KRYIAKYTIN PALAHGIAHT
VGSIEKGKLA DIVLWDPAFF GVKPALIIKG GMVAYAPMGD INAAIPTPQP VHYRPMYACL
GKAKYQTSMI FMSKAGIEAG VPEKLGLKSL IGRVEGCRHI TKASMIHNNY VPHIELDPQT
YIVKADGVPL VCEPATELPM AQRYFLF
