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P58932

- BCSA_XANAC

UniProt

P58932 - BCSA_XANAC

Protein

Cellulose synthase catalytic subunit [UDP-forming]

Gene

bcsA

Organism
Xanthomonas axonopodis pv. citri (strain 306)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (26 Jul 2002)
      Previous versions | rss
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    Functioni

    Catalytic subunit of cellulose synthase. It polymerizes uridine 5'-diphosphate glucose to cellulose, which is produced as an extracellular component for mechanical and chemical protection By similarity.By similarity

    Catalytic activityi

    UDP-glucose + (1,4-beta-D-glucosyl)(n) = UDP + (1,4-beta-D-glucosyl)(n+1).

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Activated by bis-(3'-5') cyclic diguanylic acid (c-di-GMP).By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei193 – 1931Sequence Analysis
    Binding sitei240 – 2401SubstrateSequence Analysis
    Binding sitei242 – 2421SubstrateSequence Analysis
    Active sitei337 – 3371Sequence Analysis

    GO - Molecular functioni

    1. cellulose synthase (UDP-forming) activity Source: UniProtKB-EC
    2. cyclic-di-GMP binding Source: InterPro

    GO - Biological processi

    1. cellulose biosynthetic process Source: UniProtKB-KW
    2. UDP-glucose metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Cellulose biosynthesis

    Keywords - Ligandi

    c-di-GMP

    Enzyme and pathway databases

    BioCyciXAXO190486:GH55-3518-MONOMER.
    UniPathwayiUPA00694.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cellulose synthase catalytic subunit [UDP-forming] (EC:2.4.1.12)
    Gene namesi
    Name:bcsA
    Ordered Locus Names:XAC3518
    OrganismiXanthomonas axonopodis pv. citri (strain 306)
    Taxonomic identifieri190486 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
    ProteomesiUP000000576: Chromosome

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 729729Cellulose synthase catalytic subunit [UDP-forming]PRO_0000059272Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi190486.XAC3518.

    Structurei

    3D structure databases

    ProteinModelPortaliP58932.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei30 – 5021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei110 – 13021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei171 – 19121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei405 – 42521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei427 – 44721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei520 – 54021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei549 – 56921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei610 – 63021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini575 – 67197PilZAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni151 – 24494Catalytic subdomain AAdd
    BLAST
    Regioni321 – 38161Catalytic subdomain BAdd
    BLAST

    Domaini

    There are two conserved domains in the globular part of the protein: the N-terminal domain (domain A) contains the conserved DXD motif and is possibly involved in catalysis and substrate binding. The C-terminal domain (domain B) contains the QXXRW motif and is present only in processive glycosyl transferases. It could be involved in the processivity function of the enzyme, possibly required for holding the growing glycan chain in the active site.

    Sequence similaritiesi

    Belongs to the glycosyltransferase 2 family.Curated
    Contains 1 PilZ domain.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1215.
    HOGENOMiHOG000259144.
    KOiK00694.
    OMAiQLTMGWF.
    OrthoDBiEOG66TG3C.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR003919. Cell_synth_A.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR009875. PilZ_domain.
    [Graphical view]
    PfamiPF07238. PilZ. 1 hit.
    [Graphical view]
    PRINTSiPR01439. CELLSNTHASEA.
    SUPFAMiSSF53448. SSF53448. 1 hit.
    TIGRFAMsiTIGR03030. CelA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P58932-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPLVVPHAAM PEGRLMTAAS RRSASPLPTL ATWALWLLGA LLLVFVVAVP    50
    MDVTQQLVFS GVLFAVALAV RNRGGRVVIL MMMGMSLAVS CRYIWWRMTQ 100
    TMGVGSAVDF ILGLGLLGAE LYAFVILVLG YFQVLWPLNR KPVPLPADQR 150
    LWPSVDVFIP TYNEPLSVVR TTVLAASVID WPAGKITIHL LDDGRRDEFR 200
    AFCAEVGINY VTRTNNAHAK AGNINAALKK CSGDYVAIFD CDHIPTRSFL 250
    QVAMGWFLHD TKLALVQMPH YFFSPDPFER NLDTHGKVPN EGELFYGLLQ 300
    DGNDQWNATF FCGSCAVIKR TALEEVGGVA VETVTEDAHT ALKLQRRGYR 350
    TAYLAVPQAA GLATESLSGH VAQRIRWARG MAQIARIDNP LLGRGLKLSQ 400
    RLCYLNAMLH FFYGVPRIIY LTAPLAYLFF GAHVIQASAL MILAYALPHI 450
    LQANLTNLRV QSRFRHLLWN EVYETTLAWY IFRPTLVALL NPKLGKFNVT 500
    PKGGLVARSY FDAQIAKPYL FLLLLNVVGM VAGVLRLIYV GGSGEQQTIW 550
    FNLAWTLYNM VLLGATIATA SETRQVRSAH RVPLDVPVTL YLPDGDVLPS 600
    RSVNFSTGGM AIMLAQPQPI EPGLPVQIGL SHRGVEQTLP AVVRQDRDGQ 650
    VSIQFTQMSM EQERWLVAST FARADIWLSQ WGQHDRDAFW RSMGQVLEAS 700
    ARGFGRLGGH IVDSARQGFR PRRAVDLES 729
    Length:729
    Mass (Da):80,915
    Last modified:July 26, 2002 - v1
    Checksum:iB9C08BB995E795B1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE008923 Genomic DNA. Translation: AAM38361.1.
    RefSeqiNP_643825.2. NC_003919.1.

    Genome annotation databases

    EnsemblBacteriaiAAM38361; AAM38361; XAC3518.
    GeneIDi1157589.
    KEGGixac:XAC3518.
    PATRICi24059178. VBIXanAxo33670_3640.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE008923 Genomic DNA. Translation: AAM38361.1 .
    RefSeqi NP_643825.2. NC_003919.1.

    3D structure databases

    ProteinModelPortali P58932.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 190486.XAC3518.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAM38361 ; AAM38361 ; XAC3518 .
    GeneIDi 1157589.
    KEGGi xac:XAC3518.
    PATRICi 24059178. VBIXanAxo33670_3640.

    Phylogenomic databases

    eggNOGi COG1215.
    HOGENOMi HOG000259144.
    KOi K00694.
    OMAi QLTMGWF.
    OrthoDBi EOG66TG3C.

    Enzyme and pathway databases

    UniPathwayi UPA00694 .
    BioCyci XAXO190486:GH55-3518-MONOMER.

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    InterProi IPR003919. Cell_synth_A.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR009875. PilZ_domain.
    [Graphical view ]
    Pfami PF07238. PilZ. 1 hit.
    [Graphical view ]
    PRINTSi PR01439. CELLSNTHASEA.
    SUPFAMi SSF53448. SSF53448. 1 hit.
    TIGRFAMsi TIGR03030. CelA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Comparison of the genomes of two Xanthomonas pathogens with differing host specificities."
      da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P.
      , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.
      Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 306.

    Entry informationi

    Entry nameiBCSA_XANAC
    AccessioniPrimary (citable) accession number: P58932
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 26, 2002
    Last sequence update: July 26, 2002
    Last modified: October 1, 2014
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3