Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P94571

- BCRC_BACSU

UniProt

P94571 - BCRC_BACSU

Protein

Undecaprenyl-diphosphatase BcrC

Gene

bcrC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.3 Publications

    Catalytic activityi

    Ditrans,octacis-undecaprenyl diphosphate + H2O = ditrans,octacis-undecaprenyl phosphate + phosphate.1 Publication

    GO - Molecular functioni

    1. undecaprenyl-diphosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. peptidoglycan biosynthetic process Source: UniProtKB-KW
    2. regulation of cell shape Source: UniProtKB-KW
    3. response to antibiotic Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Antibiotic resistance, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

    Enzyme and pathway databases

    BioCyciBSUB:BSU36530-MONOMER.

    Protein family/group databases

    TCDBi9.B.105.1.3. the lead resistance fusion protein (pbrbc) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Undecaprenyl-diphosphatase BcrC (EC:3.6.1.27)
    Alternative name(s):
    Undecaprenyl pyrophosphate phosphatase
    Gene namesi
    Name:bcrC
    Synonyms:ywoA
    Ordered Locus Names:BSU36530
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU36530. [Micado]

    Subcellular locationi

    Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Disruption results in a marked decrease of resistance to bacitracin.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 193193Undecaprenyl-diphosphatase BcrCPRO_0000049990Add
    BLAST

    Proteomic databases

    PaxDbiP94571.

    Expressioni

    Inductioni

    Expression is sigma M, sigma X and sigma I-dependent. Induced by vancomycin and bacitracin, via sigma M. Expression is maximal during early exponential phase and decreases during stationary phase.3 Publications

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU36530.

    Structurei

    3D structure databases

    ProteinModelPortaliP94571.
    SMRiP94571. Positions 64-161.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei24 – 4421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei53 – 7321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei119 – 13921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei140 – 16021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the BcrC/YbjG family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0671.
    HOGENOMiHOG000221066.
    OMAiRIWVGHH.
    OrthoDBiEOG661HBQ.
    PhylomeDBiP94571.

    Family and domain databases

    Gene3Di1.20.144.10. 1 hit.
    InterProiIPR000326. P_Acid_Pase_2/haloperoxidase.
    [Graphical view]
    PfamiPF01569. PAP2. 1 hit.
    [Graphical view]
    SMARTiSM00014. acidPPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF48317. SSF48317. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P94571-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNYEIFKAIH GLSHHNSVLD SIMVFITEYA IVAYALILLA IWLFGNTQSR    50
    KHVLYAGITG IAGLVINYLI TLVYFEPRPF VAHTVHTLIP HAADASFPSD 100
    HTTGALAISI AMLFRNRKIG WPLVIFGLLT GFSRIWVGHH YPVDVLGSLV 150
    VAIIIGFLFF RFSDLLRPFV DLVVRIYEAI INKLTKKPTD QNF 193
    Length:193
    Mass (Da):21,723
    Last modified:May 1, 1997 - v1
    Checksum:iE7C1ACC1556BC6CE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z82987 Genomic DNA. Translation: CAB05382.1.
    AL009126 Genomic DNA. Translation: CAB15670.1.
    PIRiD70064.
    RefSeqiNP_391534.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB15670; CAB15670; BSU36530.
    GeneIDi936946.
    KEGGibsu:BSU36530.
    PATRICi18979330. VBIBacSub10457_3827.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z82987 Genomic DNA. Translation: CAB05382.1 .
    AL009126 Genomic DNA. Translation: CAB15670.1 .
    PIRi D70064.
    RefSeqi NP_391534.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali P94571.
    SMRi P94571. Positions 64-161.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU36530.

    Protein family/group databases

    TCDBi 9.B.105.1.3. the lead resistance fusion protein (pbrbc) family.

    Proteomic databases

    PaxDbi P94571.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15670 ; CAB15670 ; BSU36530 .
    GeneIDi 936946.
    KEGGi bsu:BSU36530.
    PATRICi 18979330. VBIBacSub10457_3827.

    Organism-specific databases

    GenoListi BSU36530. [Micado ]

    Phylogenomic databases

    eggNOGi COG0671.
    HOGENOMi HOG000221066.
    OMAi RIWVGHH.
    OrthoDBi EOG661HBQ.
    PhylomeDBi P94571.

    Enzyme and pathway databases

    BioCyci BSUB:BSU36530-MONOMER.

    Family and domain databases

    Gene3Di 1.20.144.10. 1 hit.
    InterProi IPR000326. P_Acid_Pase_2/haloperoxidase.
    [Graphical view ]
    Pfami PF01569. PAP2. 1 hit.
    [Graphical view ]
    SMARTi SM00014. acidPPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48317. SSF48317. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees)."
      Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V., Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G., Kunst F., Danchin A., Glaser P.
      Microbiology 143:3313-3328(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      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.
      , 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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    3. "Regulation of the Bacillus subtilis bcrC bacitracin resistance gene by two extracytoplasmic function sigma factors."
      Cao M., Helmann J.D.
      J. Bacteriol. 184:6123-6129(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN BACITRACIN RESISTANCE, INDUCTION.
      Strain: 168 / CU1065.
    4. "YtsCD and YwoA, two independent systems that confer bacitracin resistance to Bacillus subtilis."
      Bernard R., Joseph P., Guiseppi A., Chippaux M., Denizot F.
      FEMS Microbiol. Lett. 228:93-97(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: 168.
    5. "A bacitracin-resistant Bacillus subtilis gene encodes a homologue of the membrane-spanning subunit of the Bacillus licheniformis ABC transporter."
      Ohki R., Tateno K., Okada Y., Okajima H., Asai K., Sadaie Y., Murata M., Aiso T.
      J. Bacteriol. 185:51-59(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, DISRUPTION PHENOTYPE.
      Strain: 168.
    6. "BcrC from Bacillus subtilis acts as an undecaprenyl pyrophosphate phosphatase in bacitracin resistance."
      Bernard R., El Ghachi M., Mengin-Lecreulx D., Chippaux M., Denizot F.
      J. Biol. Chem. 280:28852-28857(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
      Strain: 168.
    7. "Genetic evidence for the actin homolog gene mreBH and the bacitracin resistance gene bcrC as targets of the alternative sigma factor sigI of Bacillus subtilis."
      Tseng C.-L., Shaw G.-C.
      J. Bacteriol. 190:1561-1567(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
      Strain: 168.

    Entry informationi

    Entry nameiBCRC_BACSU
    AccessioniPrimary (citable) accession number: P94571
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 96 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Bacitracin is thought to be involved in the inhibition of peptidoglycan synthesis by sequestering undecaprenyl diphosphate, thereby reducing the pool of lipid carrier available.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3