URE2_SPOPA
ID URE2_SPOPA Reviewed; 126 AA.
AC P41021;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 114.
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 Sporosarcina pasteurii (Bacillus pasteurii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1474;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822;
RA Moersdorf G., Weinmann P., Kaltwasser H.;
RT "Nucleotide sequence of three genes on a urease encoding DNA-fragment from
RT Bacillus pasteurii.";
RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 5-126.
RX PubMed=8706719; DOI=10.1111/j.1432-1033.1996.0061u.x;
RA Benini S., Ciurli S., Nolting H.F., Mangani S.;
RT "X-ray absorption spectroscopy study of native and
RT phenylphosphorodiamidate-inhibited Bacillus pasteurii urease.";
RL Eur. J. Biochem. 239:61-66(1996).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH UREA; UREC AND
RP BETA-MERCAPTOETHANOL.
RX PubMed=9761912; DOI=10.1107/s0907444997013085;
RA Benini S., Ciurli S., Rypniewski W.R., Wilson K.S., Mangani S.;
RT "Crystallization and preliminary high-resolution X-ray diffraction analysis
RT of native and beta-mercaptoethanol-inhibited urease from Bacillus
RT pasteurii.";
RL Acta Crystallogr. D 54:409-412(1998).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH UREA; UREC AND
RP DIAMIDOPHOSPHATE.
RX PubMed=10368287; DOI=10.1016/s0969-2126(99)80026-4;
RA Benini S., Rypniewski W.R., Wilson K.S., Miletti S., Ciurli S., Mangani S.;
RT "A new proposal for urease mechanism based on the crystal structures of the
RT native and inhibited enzyme from Bacillus pasteurii: why urea hydrolysis
RT costs two nickels.";
RL Structure 7:205-216(1999).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH UREA; UREC AND
RP ACETOHYDROXAMIC ACID.
RX PubMed=10766443; DOI=10.1007/s007750050014;
RA Benini S., Rypniewski W.R., Wilson K.S., Miletti S., Ciurli S., Mangani S.;
RT "The complex of Bacillus pasteurii urease with acetohydroxamate anion from
RT X-ray data at 1.55 A resolution.";
RL J. Biol. Inorg. Chem. 5:110-118(2000).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH UREA; UREC AND
RP PHOSPHATE.
RX PubMed=11713685; DOI=10.1007/s007750100254;
RA Benini S., Rypniewski W.R., Wilson K.S., Ciurli S., Mangani S.;
RT "Structure-based rationalization of urease inhibition by phosphate: novel
RT insights into the enzyme mechanism.";
RL J. Biol. Inorg. Chem. 6:778-790(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH UREA; UREC AND BORATE
RP IONS.
RX PubMed=15038715; DOI=10.1021/ja049618p;
RA Benini S., Rypniewski W.R., Wilson K.S., Mangani S., Ciurli S.;
RT "Molecular details of urease inhibition by boric acid: insights into the
RT catalytic mechanism.";
RL J. Am. Chem. Soc. 126:3714-3715(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, ECO:0000269|PubMed:10368287,
CC ECO:0000269|PubMed:10766443, ECO:0000269|PubMed:11713685,
CC ECO:0000269|PubMed:15038715, ECO:0000269|PubMed:9761912}.
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; X78411; CAA55174.1; -; Genomic_DNA.
DR PIR; S47103; S47103.
DR PDB; 1IE7; X-ray; 1.85 A; B=1-126.
DR PDB; 1S3T; X-ray; 2.10 A; B=1-126.
DR PDB; 1UBP; X-ray; 1.65 A; B=5-126.
DR PDB; 2UBP; X-ray; 2.00 A; B=5-126.
DR PDB; 3UBP; X-ray; 2.00 A; B=1-126.
DR PDB; 4AC7; X-ray; 1.50 A; B=1-126.
DR PDB; 4CEU; X-ray; 1.58 A; B=1-126.
DR PDB; 4CEX; X-ray; 1.59 A; B=1-126.
DR PDB; 4UBP; X-ray; 1.55 A; B=1-126.
DR PDB; 5A6T; X-ray; 1.65 A; B=1-126.
DR PDB; 5FSD; X-ray; 1.75 A; B=1-126.
DR PDB; 5FSE; X-ray; 2.07 A; B=1-126.
DR PDB; 5G4H; X-ray; 1.50 A; B=1-126.
DR PDB; 5OL4; X-ray; 1.28 A; B=5-126.
DR PDB; 6G48; X-ray; 1.91 A; B=5-126.
DR PDB; 6H8J; X-ray; 1.45 A; B=5-126.
DR PDB; 6I9Y; X-ray; 2.14 A; B=5-126.
DR PDB; 6QDY; X-ray; 1.42 A; B=5-126.
DR PDB; 6RKG; X-ray; 1.32 A; B=5-126.
DR PDB; 6RP1; X-ray; 1.49 A; B=5-126.
DR PDB; 6ZNY; X-ray; 1.50 A; BBB=5-126.
DR PDB; 6ZNZ; X-ray; 1.89 A; BBB=5-126.
DR PDB; 6ZO0; X-ray; 2.23 A; BBB=5-126.
DR PDB; 6ZO1; X-ray; 1.61 A; BBB=5-126.
DR PDB; 6ZO2; X-ray; 1.65 A; BBB=5-126.
DR PDB; 6ZO3; X-ray; 1.55 A; BBB=5-126.
DR PDB; 7B58; X-ray; 1.72 A; BBB=5-126.
DR PDB; 7B59; X-ray; 1.63 A; BBB=5-126.
DR PDB; 7B5A; X-ray; 1.97 A; BBB=5-126.
DR PDBsum; 1IE7; -.
DR PDBsum; 1S3T; -.
DR PDBsum; 1UBP; -.
DR PDBsum; 2UBP; -.
DR PDBsum; 3UBP; -.
DR PDBsum; 4AC7; -.
DR PDBsum; 4CEU; -.
DR PDBsum; 4CEX; -.
DR PDBsum; 4UBP; -.
DR PDBsum; 5A6T; -.
DR PDBsum; 5FSD; -.
DR PDBsum; 5FSE; -.
DR PDBsum; 5G4H; -.
DR PDBsum; 5OL4; -.
DR PDBsum; 6G48; -.
DR PDBsum; 6H8J; -.
DR PDBsum; 6I9Y; -.
DR PDBsum; 6QDY; -.
DR PDBsum; 6RKG; -.
DR PDBsum; 6RP1; -.
DR PDBsum; 6ZNY; -.
DR PDBsum; 6ZNZ; -.
DR PDBsum; 6ZO0; -.
DR PDBsum; 6ZO1; -.
DR PDBsum; 6ZO2; -.
DR PDBsum; 6ZO3; -.
DR PDBsum; 7B58; -.
DR PDBsum; 7B59; -.
DR PDBsum; 7B5A; -.
DR AlphaFoldDB; P41021; -.
DR SMR; P41021; -.
DR BindingDB; P41021; -.
DR DrugBank; DB02899; N-Carboxymethionine.
DR BRENDA; 3.5.1.5; 682.
DR UniPathway; UPA00258; UER00370.
DR EvolutionaryTrace; P41021; -.
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..126
FT /note="Urease subunit beta"
FT /id="PRO_0000067569"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:5OL4"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 27..34
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:5OL4"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:5OL4"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:5OL4"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:5OL4"
FT HELIX 110..120
FT /evidence="ECO:0007829|PDB:5OL4"
SQ SEQUENCE 126 AA; 13959 MW; E1BE8E5209586B02 CRC64;
MSNNNYIVPG EYRVAEGEIE INAGREKTTI RVSNTGDRPI QVGSHIHFVE VNKELLFDRA
EGIGRRLNIP SGTAARFEPG EEMEVELTEL GGNREVFGIS DLTNGSVDNK ELILQRAKEL
GYKGVE
