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P77837 (URE1_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Urease subunit alpha
EC=3.5.1.5
Alternative name(s):
Urea amidohydrolase subunit alpha
Gene names
Name:ureC
Ordered Locus Names:BSU36640
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length569 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Urea + H2O = CO2 + 2 NH3. Ref.1 Ref.3

Cofactor

Binds 2 nickel ions per subunit By similarity. HAMAP MF_01953

Pathway

Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. HAMAP MF_01953

Subunit structure

Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to form the active enzyme By similarity.

Subcellular location

Cytoplasm By similarity HAMAP MF_01953.

Post-translational modification

Carbamylation allows a single lysine to coordinate two nickel ions By similarity. HAMAP MF_01953

Sequence similarities

Belongs to the urease family.

Contains 1 urease domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Nickel
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processurea metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionnickel cation binding

Inferred from electronic annotation. Source: InterPro

urease activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 569569Urease subunit alpha HAMAP MF_01953
PRO_0000067538

Regions

Domain132 – 569438Urease

Sites

Active site3231Proton donor By similarity
Metal binding1371Nickel 2 By similarity
Metal binding1391Nickel 2 By similarity
Metal binding2201Nickel 1; via carbamate group By similarity
Metal binding2201Nickel 2; via carbamate group By similarity
Metal binding2491Nickel 1 By similarity
Metal binding2751Nickel 1 By similarity
Metal binding3631Nickel 2 By similarity
Binding site2221Substrate By similarity

Amino acid modifications

Modified residue2201N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P77837 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: A2712A6172DA5BE7

FASTA56961,187
        10         20         30         40         50         60 
MKMSREEYAE LFGPTTGDKI RLGDTDLWIE VEKDFTVYGE EMIFGGGKTI RDGMGQNGRI 

        70         80         90        100        110        120 
TGKDGALDLV ITNVVLLDYT GIVKADVGVK DGRIVGVGKS GNPDIMDGVD PHMVIGAGTE 

       130        140        150        160        170        180 
VISGEGKILT AGGVDTHIHF ICPQQMEVAL SSGVTTLLGG GTGPATGSKA TTCTSGAWYM 

       190        200        210        220        230        240 
ARMLEAAEEF PINVGFLGKG NASDKAPLIE QVEAGAIGLK LHEDWGTTPS AIKTCMEVVD 

       250        260        270        280        290        300 
EADIQVAIHT DTINEAGFLE NTLDAIGDRV IHTYHIEGAG GGHAPDIMKL ASYANILPSS 

       310        320        330        340        350        360 
TTPTIPYTVN TMDEHLDMMM VCHHLDAKVP EDVAFSHSRI RAATIAAEDI LHDIGAISMT 

       370        380        390        400        410        420 
SSDSQAMGRV GEVIIRTWQV ADKMKKQRGA LAGENGNDNV RAKRYIAKYT INPAITHGLS 

       430        440        450        460        470        480 
HEVGSVEKGK LADLVLWDPV FFGVKPELVL KGGMIARAQM GDPNASIPTP EPVFMRQMYA 

       490        500        510        520        530        540 
SYGKANRSTS ITFMSQASIE RGVAESLGLE KRISPVKNIR KLSKLDMKLN SALPKIEIDP 

       550        560 
KTYQVFADGE ELSCQPVDYV PLGQRYFLF

« Hide

References

« Hide 'large scale' references
[1]"The Bacillus subtilis ureABC operon."
Cruz-Ramos H., Glaser P., Wray L.V. Jr., Fisher S.H.
J. Bacteriol. 179:3371-3373(1997) [PubMed: 9150240] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY.
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Biosynthesis of active Bacillus subtilis urease in the absence of known urease accessory proteins."
Kim J.K., Mulrooney S.B., Hausinger R.P.
J. Bacteriol. 187:7150-7154(2005) [PubMed: 16199586] [Abstract]
Cited for: CATALYTIC ACTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y08559 Genomic DNA. Translation: CAA69859.1.
AL009126 Genomic DNA. Translation: CAB15681.1.
PIRD69729.
RefSeqNP_391545.1. NC_000964.3.

3D structure databases

ProteinModelPortalP77837.
SMRP77837. Positions 3-569.
ModBaseSearch...

Protein family/group databases

MEROPSM38.982.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000001037; EBBACP00000001037; EBBACG00000001035.
GeneID936958.
GenomeReviewsGene locus BSU36640 in contig AL009126_GR.
KEGGbsu:BSU36640.
NMPDRfig|224308.1.peg.3671.
PATRIC18979356. VBIBacSub10457_3840.

Organism-specific databases

GenoListBSU36640. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000002324.
HOGENOMHBG357507.
OMATIHAFHT.
PhylomeDBP77837.
ProtClustDBPRK13207.

Enzyme and pathway databases

BioCycBSUB:BSU36640-MONOMER.

Family and domain databases

HAMAPMF_01953. Urease_alpha.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR011059. Metal-dep_hydrolase_composite.
IPR011612. Urease_alpha_N.
IPR005848. Urease_asu.
IPR017951. Urease_asu_c.
IPR017950. Urease_asu_CS.
[Graphical view]
KOK01428.
PfamPF01979. Amidohydro_1. 1 hit.
PF00449. Urease_alpha. 1 hit.
[Graphical view]
PRINTSPR01752. UREASE.
SUPFAMSSF51338. Metalo_hydrolase. 2 hits.
TIGRFAMsTIGR01792. Urease_alph. 1 hit.
PROSITEPS01120. UREASE_1. 1 hit.
PS00145. UREASE_2. 1 hit.
PS51368. UREASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameURE1_BACSU
AccessionPrimary (citable) accession number: P77837
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: January 25, 2012
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents