URE1_STRE5
ID URE1_STRE5 Reviewed; 572 AA.
AC P50047; F8HGK0; Q59970;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 3.
DT 03-AUG-2022, entry version 126.
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=Ssal_01900;
OS Streptococcus salivarius (strain 57.I).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1046629;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=57.I;
RX PubMed=8550211; DOI=10.1128/iai.64.2.585-592.1996;
RA Chen Y.-Y.M., Clancy K.A., Burne R.A.;
RT "Streptococcus salivarius urease: genetic and biochemical characterization
RT and expression in a dental plaque streptococcus.";
RL Infect. Immun. 64:585-592(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=57.I;
RX PubMed=21914897; DOI=10.1128/jb.05670-11;
RA Geng J., Huang S.C., Li S., Hu S., Chen Y.Y.;
RT "Complete genome sequence of the ureolytic Streptococcus salivarius strain
RT 57.I.";
RL J. Bacteriol. 193:5596-5597(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 228-409, AND INDUCTION.
RC STRAIN=57.I;
RX PubMed=8595861; DOI=10.1111/j.1574-6968.1996.tb07993.x;
RA Chen Y.-Y.M., Burne R.A.;
RT "Analysis of Streptococcus salivarius urease expression using continuous
RT chemostat culture.";
RL FEMS Microbiol. Lett. 135:223-229(1996).
RN [4]
RP INDUCTION.
RC STRAIN=57.I;
RX PubMed=9791132; DOI=10.1128/jb.180.21.5769-5775.1998;
RA Chen Y.-Y.M., Weaver C.A., Mendelsohn D.R., Burne R.A.;
RT "Transcriptional regulation of the Streptococcus salivarius 57.I urease
RT operon.";
RL J. Bacteriol. 180:5769-5775(1998).
RN [5]
RP FUNCTION.
RC STRAIN=57.I;
RX PubMed=10913107; DOI=10.1128/jb.182.16.4667-4669.2000;
RA Chen Y.-Y.M., Weaver C.A., Burne R.A.;
RT "Dual functions of Streptococcus salivarius urease.";
RL J. Bacteriol. 182:4667-4669(2000).
CC -!- FUNCTION: Ureolysis may allow urea to be employed as a nitrogen source
CC for growth and produces ammonia which may protect from killing at low
CC pH. {ECO:0000269|PubMed:10913107}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.7 mM for urea (at pH 7.0 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:8550211};
CC Note=Urea concentrations in the oral cavity of humans normally range
CC from 3 mM to 10 mM.;
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:8550211};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:8550211};
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 -!- INDUCTION: By low pH and excess glucose. {ECO:0000269|PubMed:8595861,
CC ECO:0000269|PubMed:9791132}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEJ54136.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U35248; AAC43564.1; -; Genomic_DNA.
DR EMBL; CP002888; AEJ54136.1; ALT_INIT; Genomic_DNA.
DR EMBL; U22950; AAB01507.1; -; Genomic_DNA.
DR AlphaFoldDB; P50047; -.
DR SMR; P50047; -.
DR STRING; 1046629.Ssal_01900; -.
DR MEROPS; M38.982; -.
DR EnsemblBacteria; AEJ54136; AEJ54136; Ssal_01900.
DR KEGG; stf:Ssal_01900; -.
DR PATRIC; fig|1046629.4.peg.1686; -.
DR eggNOG; COG0804; Bacteria.
DR BioCyc; MetaCyc:MON-182; -.
DR SABIO-RK; P50047; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000000293; 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 Cytoplasm; Hydrolase; Metal-binding; Nickel.
FT CHAIN 1..572
FT /note="Urease subunit alpha"
FT /id="PRO_0000067561"
FT DOMAIN 133..572
FT /note="Urease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT ACT_SITE 324
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 138
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 140
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 221
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 221
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 223
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 250
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 276
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 364
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 221
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT CONFLICT 305
FT /note="T -> I (in Ref. 1; AAC43564 and 3; AAB01507)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 572 AA; 61812 MW; E390DB1B7EC8032E CRC64;
MSFKMDREEY AQHYGPTVGD SVRLGDTNLF AAIEKDFTVY GQESKFGGGK VLRDGMGVSA
TETRDNPSVV DTIITGATII DYTGIIKADI GIRDGKIVAI GRGGNPDTMD NVDFVVGAST
EAIAAEGLIV TAGGIDLHVH YISADLPEFG LDNGITTLFG GGTGPADGSN ATTCTPGKFH
ITRMLQAVDD MPANFGFLAK GVGSETEVVE EQIKAGAAGI KTHEDWGATY AGIDNSLKVA
DKYDVSFAVH TDSLNEGGFM ENTLESFQGR TVHTFHTEGS GGGHAPDIMV FAGKENILPS
STNPTNPYTT NAIGELLDMV MVCHHLDPKI PEDVSFAESR VRKQTVAAED VLHDMGALSI
MTSDAMAMGR VGEVAMRCWQ LADKMKAQRG PLEGDSEFND NNRIKRYVAK YTINPAITNG
IADYIGSVEV GKFADLVIWE PAQFGAKPKL VLKGGMLTYG VMGDAGSSLP TPQPRIMRKL
YGAYGQAVHE TNLTFVSQYA YDHGIKEEIG LNKIVLPVKN TRNLTKRDMK LNDYAPKTIR
IDPQTFDVFI DDELVTCEPI HTTSLSQRYF LF
