URE2_CORGL
ID URE2_CORGL Reviewed; 162 AA.
AC Q79VJ4; Q9L421; Q9RHM5;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Urease subunit beta {ECO:0000255|HAMAP-Rule:MF_01954};
DE EC=3.5.1.5 {ECO:0000255|HAMAP-Rule:MF_01954};
DE AltName: Full=Urea amidohydrolase subunit beta {ECO:0000255|HAMAP-Rule:MF_01954};
GN Name=ureB {ECO:0000255|HAMAP-Rule:MF_01954};
GN OrderedLocusNames=Cgl0085, cg0114;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC 13869 / DSMZ 1412 / NCIMB 9567;
RX PubMed=11328647; DOI=10.3109/10425170009033989;
RA Puskas L.G., Inui M., Yukawa H.;
RT "Structure of the urease operon of Corynebacterium glutamicum.";
RL DNA Seq. 11:383-394(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND OPERON STRUCTURE.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=10930756; DOI=10.1111/j.1574-6968.2000.tb09248.x;
RA Nolden L., Beckers G., Moeckel B., Pfefferle W., Nampoothiri K.M.,
RA Kraemer R., Burkovski A.;
RT "Urease of Corynebacterium glutamicum: organization of corresponding genes
RT and investigation of activity.";
RL FEMS Microbiol. Lett. 189:305-310(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [5]
RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15516578; DOI=10.1128/jb.186.22.7645-7652.2004;
RA Beckers G., Bendt A.K., Kraemer R., Burkovski A.;
RT "Molecular identification of the urea uptake system and transcriptional
RT analysis of urea transporter- and urease-encoding genes in Corynebacterium
RT glutamicum.";
RL J. Bacteriol. 186:7645-7652(2004).
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_01954};
CC -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC urea (urease route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01954}.
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_01954}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01954}.
CC -!- INDUCTION: By urea and nitrogen starvation.
CC {ECO:0000269|PubMed:11328647, ECO:0000269|PubMed:15516578}.
CC -!- SIMILARITY: Belongs to the urease beta subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01954}.
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DR EMBL; AB029154; BAA88553.1; -; Genomic_DNA.
DR EMBL; AJ251883; CAB81936.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB97478.1; -; Genomic_DNA.
DR EMBL; BX927148; CAF18653.1; -; Genomic_DNA.
DR RefSeq; NP_599337.1; NC_003450.3.
DR RefSeq; WP_011013377.1; NC_006958.1.
DR AlphaFoldDB; Q79VJ4; -.
DR SMR; Q79VJ4; -.
DR STRING; 196627.cg0114; -.
DR KEGG; cgb:cg0114; -.
DR KEGG; cgl:Cgl0085; -.
DR PATRIC; fig|196627.13.peg.86; -.
DR eggNOG; COG0832; Bacteria.
DR HOGENOM; CLU_129707_1_0_11; -.
DR OMA; FYEVNDA; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0035550; C:urease complex; IEA:InterPro.
DR GO; GO:0009039; F:urease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00407; Urease_beta; 1.
DR Gene3D; 2.10.150.10; -; 1.
DR HAMAP; MF_01954; Urease_beta; 1.
DR InterPro; IPR002019; Urease_beta.
DR InterPro; IPR036461; Urease_betasu_sf.
DR Pfam; PF00699; Urease_beta; 1.
DR SUPFAM; SSF51278; SSF51278; 1.
DR TIGRFAMs; TIGR00192; urease_beta; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..162
FT /note="Urease subunit beta"
FT /id="PRO_0000234246"
FT REGION 116..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 103..105
FT /note="DLK -> TQ (in Ref. 1; BAA88553)"
FT /evidence="ECO:0000305"
FT CONFLICT 110..131
FT /note="EGREDGWRRSSAAGDAPQELPQ -> RTEDDGVVLSCCDVHKIAT (in
FT Ref. 1; BAA88553)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="G -> A (in Ref. 1; BAA88553)"
FT /evidence="ECO:0000305"
FT CONFLICT 147..148
FT /note="VD -> AN (in Ref. 1; BAA88553)"
FT /evidence="ECO:0000305"
FT CONFLICT 157..160
FT /note="Missing (in Ref. 1; BAA88553)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 162 AA; 17568 MW; FAB0C50E993F8C25 CRC64;
MIPGEYILSS ESLTGNVGRE AKTIEIINTG DRPVQIGSHF HFAEVNPSIS FDRSEGYGFR
LDIPSGTAVR LEPGDARTVN LVAIGGDRIV AGFRDLVDGP LEDLKVNVWE GREDGWRRSS
AAGDAPQELP QVEAAERGRK LDDATDVDTN VGTEEGFEEG RN
