URE2_KLEAE
ID URE2_KLEAE Reviewed; 106 AA.
AC P18315;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 25-MAY-2022, entry version 129.
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};
OS Klebsiella aerogenes (Enterobacter aerogenes).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=548;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC STRAIN=CG253;
RX PubMed=2211515; DOI=10.1128/jb.172.10.5837-5843.1990;
RA Mulrooney S.B., Hausinger R.P.;
RT "Sequence of the Klebsiella aerogenes urease genes and evidence for
RT accessory proteins facilitating nickel incorporation.";
RL J. Bacteriol. 172:5837-5843(1990).
RN [2]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=1400317; DOI=10.1016/s0021-9258(19)88659-3;
RA Martin P.R., Hausinger R.P.;
RT "Site-directed mutagenesis of the active site cysteine in Klebsiella
RT aerogenes urease.";
RL J. Biol. Chem. 267:20024-20027(1992).
RN [3]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP HIS-39 AND HIS-41.
RX PubMed=8318888; DOI=10.1002/pro.5560020616;
RA Park I.-S., Hausinger R.P.;
RT "Site-directed mutagenesis of Klebsiella aerogenes urease: identification
RT of histidine residues that appear to function in nickel ligation, substrate
RT binding, and catalysis.";
RL Protein Sci. 2:1034-1041(1993).
RN [4]
RP CATALYTIC ACTIVITY, AND INTERACTION WITH UREA; UREC AND URED.
RX PubMed=7909161; DOI=10.1073/pnas.91.8.3233;
RA Park I.-S., Carr M.B., Hausinger R.P.;
RT "In vitro activation of urease apoprotein and role of UreD as a chaperone
RT required for nickel metallocenter assembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:3233-3237(1994).
RN [5]
RP CATALYTIC ACTIVITY, AND INTERACTION WITH UREA; UREC; URED; UREF AND UREG.
RX PubMed=7721685; DOI=10.1128/jb.177.8.1947-1951.1995;
RA Park I.-S., Hausinger R.P.;
RT "Evidence for the presence of urease apoprotein complexes containing UreD,
RT UreF, and UreG in cells that are competent for in vivo enzyme activation.";
RL J. Bacteriol. 177:1947-1951(1995).
RN [6]
RP CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=7855593; DOI=10.1126/science.7855593;
RA Park I.-S., Hausinger R.P.;
RT "Requirement of carbon dioxide for in vitro assembly of the urease nickel
RT metallocenter.";
RL Science 267:1156-1158(1995).
RN [7]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND INTERACTION WITH UREA; UREC;
RP URED AND UREF.
RX PubMed=8808930; DOI=10.1128/jb.178.18.5417-5421.1996;
RA Moncrief M.B.C., Hausinger R.P.;
RT "Purification and activation properties of UreD-UreF-urease apoprotein
RT complexes.";
RL J. Bacteriol. 178:5417-5421(1996).
RN [8]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND INTERACTION WITH UREA; UREC;
RP URED; UREF AND UREG.
RX PubMed=10500143; DOI=10.1073/pnas.96.20.11140;
RA Soriano A., Hausinger R.P.;
RT "GTP-dependent activation of urease apoprotein in complex with the UreD,
RT UreF, and UreG accessory proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11140-11144(1999).
RN [9]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND ACTIVATION OF THE APOPROTEIN
RP BY UREE.
RX PubMed=11015224; DOI=10.1021/bi001296o;
RA Soriano A., Colpas G.J., Hausinger R.P.;
RT "UreE stimulation of GTP-dependent urease activation in the UreD-UreF-UreG-
RT urease apoprotein complex.";
RL Biochemistry 39:12435-12440(2000).
RN [10]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11594743; DOI=10.1006/abbi.2001.2536;
RA Mulrooney S.B., Zakharian T., Schaller R.A., Hausinger R.P.;
RT "Dual effects of ionic strength on Klebsiella aerogenes urease: pH-
RT dependent activation and inhibition.";
RL Arch. Biochem. Biophys. 394:280-282(2001).
RN [11]
RP INTERACTION WITH UREA; UREC; URED AND UREF, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=14749331; DOI=10.1074/jbc.m312979200;
RA Chang Z., Kuchar J., Hausinger R.P.;
RT "Chemical cross-linking and mass spectrometric identification of sites of
RT interaction for UreD, UreF, and urease.";
RL J. Biol. Chem. 279:15305-15313(2004).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH UREA AND UREC.
RX PubMed=7754395; DOI=10.1126/science.7754395;
RA Jabri E., Carr M.B., Hausinger R.P., Karplus P.A.;
RT "The crystal structure of urease from Klebsiella aerogenes.";
RL Science 268:998-1004(1995).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH UREA AND UREC.
RX PubMed=8718850; DOI=10.1021/bi960424z;
RA Jabri E., Karplus P.A.;
RT "Structures of the Klebsiella aerogenes urease apoenzyme and two active-
RT site mutants.";
RL Biochemistry 35:10616-10626(1996).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH UREA AND UREC.
RX PubMed=8702515; DOI=10.1074/jbc.271.31.18632;
RA Park I.-S., Michel L.O., Pearson M.A., Jabri E., Karplus P.A., Wang S.,
RA Dong J., Scott R.A., Koehler B.P., Johnson M.K., Hausinger R.P.;
RT "Characterization of the mononickel metallocenter in H134A mutant urease.";
RL J. Biol. Chem. 271:18632-18637(1996).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH UREA; UREC AND
RP ACETOHYDROXAMIC ACID.
RX PubMed=9201965; DOI=10.1021/bi970514j;
RA Pearson M.A., Michel L.O., Hausinger R.P., Karplus P.A.;
RT "Structures of Cys319 variants and acetohydroxamate-inhibited Klebsiella
RT aerogenes urease.";
RL Biochemistry 36:8164-8172(1997).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-101 IN COMPLEX WITH UREA; UREC
RP AND FORMATE.
RX PubMed=9558361; DOI=10.1021/bi980021u;
RA Pearson M.A., Schaller R.A., Michel L.O., Karplus P.A., Hausinger R.P.;
RT "Chemical rescue of Klebsiella aerogenes urease variants lacking the
RT carbamylated-lysine nickel ligand.";
RL Biochemistry 37:6214-6220(1998).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-101 IN COMPLEX WITH UREA AND
RP UREC.
RX PubMed=10555581; DOI=10.1007/s007750050333;
RA Yamaguchi K., Cosper N.J., Staalhandske C., Scott R.A., Pearson M.A.,
RA Karplus P.A., Hausinger R.P.;
RT "Characterization of metal-substituted Klebsiella aerogenes urease.";
RL J. Biol. Inorg. Chem. 4:468-477(1999).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-101 IN COMPLEX WITH UREA AND
RP UREC, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10913264; DOI=10.1021/bi000613o;
RA Pearson M.A., Park I.-S., Schaller R.A., Michel L.O., Karplus P.A.,
RA Hausinger R.P.;
RT "Kinetic and structural characterization of urease active site variants.";
RL Biochemistry 39:8575-8584(2000).
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 ECO:0000269|PubMed:10500143, ECO:0000269|PubMed:11015224,
CC ECO:0000269|PubMed:1400317, ECO:0000269|PubMed:2211515,
CC ECO:0000269|PubMed:7721685, ECO:0000269|PubMed:7855593,
CC ECO:0000269|PubMed:7909161, ECO:0000269|PubMed:8318888,
CC ECO:0000269|PubMed:8808930};
CC -!- ACTIVITY REGULATION: The apoenzyme can be activated in vitro in the
CC presence of nickel ions and carbon dioxide, which promotes
CC carboxylation of 'Lys-217' of the UreC (alpha) subunit.
CC {ECO:0000269|PubMed:10500143, ECO:0000269|PubMed:11015224,
CC ECO:0000269|PubMed:7855593, ECO:0000269|PubMed:8808930}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.3 mM for urea {ECO:0000269|PubMed:10913264,
CC ECO:0000269|PubMed:11594743, ECO:0000269|PubMed:1400317,
CC ECO:0000269|PubMed:8318888};
CC Vmax=1.9 mmol/min/mg enzyme {ECO:0000269|PubMed:10913264,
CC ECO:0000269|PubMed:11594743, ECO:0000269|PubMed:1400317,
CC ECO:0000269|PubMed:8318888};
CC pH dependence:
CC Optimum pH is 7.75. {ECO:0000269|PubMed:10913264,
CC ECO:0000269|PubMed:11594743, ECO:0000269|PubMed:1400317,
CC ECO:0000269|PubMed:8318888};
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. The
CC apoenzyme interacts with an accessory complex composed of UreD, UreF
CC and UreG, which is required for the assembly of the nickel containing
CC metallocenter of UreC. The UreE protein may also play a direct role as
CC a metallochaperone in nickel transfer to the urease apoprotein.
CC {ECO:0000255|HAMAP-Rule:MF_01954, ECO:0000269|PubMed:10500143,
CC ECO:0000269|PubMed:10555581, ECO:0000269|PubMed:10913264,
CC ECO:0000269|PubMed:14749331, ECO:0000269|PubMed:7721685,
CC ECO:0000269|PubMed:7754395, ECO:0000269|PubMed:7909161,
CC ECO:0000269|PubMed:8702515, ECO:0000269|PubMed:8718850,
CC ECO:0000269|PubMed:8808930, ECO:0000269|PubMed:9201965,
CC ECO:0000269|PubMed:9558361}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01954}.
CC -!- SIMILARITY: Belongs to the urease beta subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01954}.
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DR EMBL; M36068; AAA25150.1; -; Genomic_DNA.
DR RefSeq; WP_002916872.1; NZ_LR134254.1.
DR PDB; 1A5K; X-ray; 2.20 A; B=1-101.
DR PDB; 1A5L; X-ray; 2.20 A; B=1-101.
DR PDB; 1A5M; X-ray; 2.00 A; B=1-101.
DR PDB; 1A5N; X-ray; 2.40 A; B=1-101.
DR PDB; 1A5O; X-ray; 2.50 A; B=1-101.
DR PDB; 1EF2; X-ray; 2.50 A; B=1-101.
DR PDB; 1EJR; X-ray; 2.00 A; B=1-101.
DR PDB; 1EJS; X-ray; 2.00 A; B=1-101.
DR PDB; 1EJT; X-ray; 2.00 A; B=1-101.
DR PDB; 1EJU; X-ray; 2.00 A; B=1-101.
DR PDB; 1EJV; X-ray; 2.40 A; B=1-101.
DR PDB; 1EJW; X-ray; 1.90 A; B=1-101.
DR PDB; 1EJX; X-ray; 1.60 A; B=1-101.
DR PDB; 1FWA; X-ray; 2.00 A; B=1-106.
DR PDB; 1FWB; X-ray; 2.00 A; B=1-106.
DR PDB; 1FWC; X-ray; 2.00 A; B=1-106.
DR PDB; 1FWD; X-ray; 2.00 A; B=1-106.
DR PDB; 1FWE; X-ray; 2.00 A; B=1-106.
DR PDB; 1FWF; X-ray; 2.00 A; B=1-106.
DR PDB; 1FWG; X-ray; 2.00 A; B=1-106.
DR PDB; 1FWH; X-ray; 2.00 A; B=1-106.
DR PDB; 1FWI; X-ray; 2.00 A; B=1-106.
DR PDB; 1FWJ; X-ray; 2.20 A; B=1-106.
DR PDB; 1KRA; X-ray; 2.30 A; B=1-106.
DR PDB; 1KRB; X-ray; 2.50 A; B=1-106.
DR PDB; 1KRC; X-ray; 2.50 A; B=1-106.
DR PDB; 2KAU; X-ray; 2.00 A; B=1-106.
DR PDB; 4EP8; X-ray; 1.55 A; B=1-101.
DR PDB; 4EPB; X-ray; 1.75 A; B=1-101.
DR PDB; 4EPD; X-ray; 1.70 A; B=1-101.
DR PDB; 4EPE; X-ray; 2.05 A; B=1-101.
DR PDBsum; 1A5K; -.
DR PDBsum; 1A5L; -.
DR PDBsum; 1A5M; -.
DR PDBsum; 1A5N; -.
DR PDBsum; 1A5O; -.
DR PDBsum; 1EF2; -.
DR PDBsum; 1EJR; -.
DR PDBsum; 1EJS; -.
DR PDBsum; 1EJT; -.
DR PDBsum; 1EJU; -.
DR PDBsum; 1EJV; -.
DR PDBsum; 1EJW; -.
DR PDBsum; 1EJX; -.
DR PDBsum; 1FWA; -.
DR PDBsum; 1FWB; -.
DR PDBsum; 1FWC; -.
DR PDBsum; 1FWD; -.
DR PDBsum; 1FWE; -.
DR PDBsum; 1FWF; -.
DR PDBsum; 1FWG; -.
DR PDBsum; 1FWH; -.
DR PDBsum; 1FWI; -.
DR PDBsum; 1FWJ; -.
DR PDBsum; 1KRA; -.
DR PDBsum; 1KRB; -.
DR PDBsum; 1KRC; -.
DR PDBsum; 2KAU; -.
DR PDBsum; 4EP8; -.
DR PDBsum; 4EPB; -.
DR PDBsum; 4EPD; -.
DR PDBsum; 4EPE; -.
DR AlphaFoldDB; P18315; -.
DR SMR; P18315; -.
DR IntAct; P18315; 2.
DR MEROPS; M38.982; -.
DR BRENDA; 3.5.1.5; 152.
DR SABIO-RK; P18315; -.
DR UniPathway; UPA00258; UER00370.
DR EvolutionaryTrace; P18315; -.
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 3D-structure; Cytoplasm; Hydrolase.
FT CHAIN 1..106
FT /note="Urease subunit beta"
FT /id="PRO_0000067577"
FT MUTAGEN 39
FT /note="H->A: Reduces activity by 20% and reduces thermal
FT stability above 50 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:8318888"
FT MUTAGEN 41
FT /note="H->A: Reduces activity by 30% and reduces thermal
FT stability above 50 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:8318888"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 21..28
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:4EP8"
FT TURN 53..58
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:4EP8"
SQ SEQUENCE 106 AA; 11695 MW; A232BFCD74864EA6 CRC64;
MIPGEYHVKP GQIALNTGRA TCRVVVENHG DRPIQVGSHY HFAEVNPALK FDRQQAAGYR
LNIPAGTAVR FEPGQKREVE LVAFAGHRAV FGFRGEVMGP LEVNDE
