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UniProtKB/Swiss-Prot entry P37467


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name XPAC_BACSU
Primary accession number P37467
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1994
Sequence was last modified on October 1, 1994 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 48)
Name and origin of the protein
Protein name Protein xpaC
Synonyms None
Gene name
Name: xpaC
OrderedLocusNames: BSU00250
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 4: Predicted;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
Bookstein C., Edwards C.W., Hulett F.M.;
"Characterization of the Bacillus subtilis xpaC gene, which in double copy causes aberrant cell morphology, filamentation and inhibits sporulation.";
Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
DOI=10.1093/dnares/1.1.1; PubMed=7584024 [NCBI, ExPASy, EBI, Israel, Japan]
Ogasawara N., Nakai S., Yoshikawa H.;
"Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin.";
DNA Res. 1:1-14(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
Comments
  • FUNCTION: In double copy it causes aberrant cell morphology, filamentation and inhibits sporulation. Hydrolyzes 5-bromo-4-chloroindolyl phosphate.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M96156; AAA22891.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D26185; BAA05261.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL009126; CAB11801.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S27526; S27526.
RefSeq NP_387906.1; -.
3D structure databases
ModBase P37467.
Enzyme and pathway databases
BioCyc BSUB224308:BSU0025-MON; -.
Organism-specific databases
SubtiList BG10089; xpaC. [Micado]
Ontologies
GO
GO:0016787; Molecular function: hydrolase activity (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR018770; Halogen_hydrol.
Graphical view of domain structure.
Pfam PF10112; Halogen_Hydrol; 1.
Pfam graphical view of domain structure.
Genome annotation databases
GeneID 937019; -.
GenomeReviews AL009126_GR; BSU00250.
KEGG bsu:BSU00250; -.
NMPDR fig|224308.1.peg.25; -.
Phylogenomic databases
HOGENOM P37467; -.
OMA P37467; MRYNISR.
Genome annotation databases
CMR P37467; BSU00250.
Other
ProtoNet P37467.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Hydrolase.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   204  204     Protein xpaC. PRO_0000066038
Sequence information
Length: 204 AA [This is the length of the unprocessed precursor] Molecular weight: 23959 Da [This is the MW of the unprocessed precursor] CRC64: 1A77046FCE60955E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MQRFFHFLVW SLTSSATFVF IGILSFFGLN QSIFLSIVYG LASGAAVYIA GIWNARRLFL 

        70         80         90        100        110        120 
KKHELTGREY AYIKKNLEEA RQKMVRLRKA LFQAKSIQMF KQNAEMLRIV RRIYLLTKKE 

       130        140        150        160        170        180 
PKRFYQAERF FYQTLDSVVE LTEKYAFLSS HPKKSKELSM SLSETRITLT ELTKRLEEDL 

       190        200 
TQAMGDEIDE LQFELDAAKH SLKK 

P37467 in FASTA format

View entry in raw text format (no links)
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