URE12_BRUSU
ID URE12_BRUSU Reviewed; 573 AA.
AC Q8FZW2; G0KB43;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Urease subunit alpha 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01953};
GN Name=ureC2 {ECO:0000255|HAMAP-Rule:MF_01953};
GN OrderedLocusNames=BR1358, BS1330_I1353;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
RN [3]
RP OPERON DISRUPTION, AND LACK OF ROLE IN VIRULENCE.
RC STRAIN=1330;
RX PubMed=17578575; DOI=10.1186/1471-2180-7-57;
RA Bandara A.B., Contreras A., Contreras-Rodriguez A., Martins A.M.,
RA Dobrean V., Poff-Reichow S., Rajasekaran P., Sriranganathan N.,
RA Schurig G.G., Boyle S.M.;
RT "Brucella suis urease encoded by ure1 but not ure2 is necessary for
RT intestinal infection of BALB/c mice.";
RL BMC Microbiol. 7:57-57(2007).
CC -!- FUNCTION: Disrupting the ure2 operon has no effect on urease activity,
CC or pathogen survival in BALB/c mice when inoculated by gavage, but
CC confers slightly enhanced resistance to low pH killing in vitro.
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; AE014291; AAN30272.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM18689.1; -; Genomic_DNA.
DR RefSeq; WP_004690958.1; NZ_KN046804.1.
DR AlphaFoldDB; Q8FZW2; -.
DR SMR; Q8FZW2; -.
DR MEROPS; M38.982; -.
DR EnsemblBacteria; AEM18689; AEM18689; BS1330_I1353.
DR GeneID; 45052378; -.
DR GeneID; 55591018; -.
DR KEGG; bms:BR1358; -.
DR KEGG; bsi:BS1330_I1353; -.
DR PATRIC; fig|204722.22.peg.318; -.
DR HOGENOM; CLU_000980_0_0_5; -.
DR OMA; CHHLSHD; -.
DR PhylomeDB; Q8FZW2; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000007104; Chromosome I.
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; IPR001763; Rhodanese-like_dom.
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.
FT CHAIN 1..573
FT /note="Urease subunit alpha 2"
FT /id="PRO_0000234146"
FT DOMAIN 135..573
FT /note="Urease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT ACT_SITE 326
FT /note="Proton donor"
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 142
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 223
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 223
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 225
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 252
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 278
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 366
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 223
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
SQ SEQUENCE 573 AA; 60720 MW; A03091E004BA75CE CRC64;
MTQISRQQYA DLYGPTIGDK IRLGDSDLYV EIEKDLRATY GDELQYGGGK TLRDGMGSEN
FLTQEAGCLD LVITNVTVID AIQGVVKADV GIRNGRIVGL GKAGNPSTMD GVTRGLVTGA
STDAISGEHL ILTAGGMDTH VHYIAPQQVE AALSNGITTL WGGGIGPVDG TNGVTTTNGP
WNLEMMLRSI EGLPINFGIQ GKGNSTGIAP LIEHLEAGAA GFKVHEDYGA TPAAIRACLS
VADEYDVSVA VHTDTLNESG YVEDTIAAFD GRSVHTYHSE GAGGGHAPDL LKVVGQNNIL
PSSTNPTLPC GKNSVAELFD MIMVCHNLNP KIPSDVAFAE SRVRAETIVA ESVLHDMGAI
SMIGSDSQAM GRIGETFLRA IQTADAMKKA RGPLPEDAPG NDNFRVLRYI AKVTINPALT
AGVGDVIGSI ESGKFADLVL WEPAFFGVKP KLVLKGGLVA WANMGDPNAS LPTPQPMYYR
PMFAAYGSAL QKTSITFVSR AAYDKGVADR FGLQRLVMPV SGTRVIGKAH MVRNSYLPNI
EVDPQTFAVK VDGVHATVKP PQSISLNQLY FFS
