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Protein

Cellulose synthase catalytic subunit [UDP-forming]

Gene

bcsA

Organism
Xanthomonas axonopodis pv. citri (strain 306)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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

Mg2+By similarity

Enzyme regulationi

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

Pathway: bacterial cellulose biosynthesis

This protein is involved in the pathway bacterial cellulose biosynthesis, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway bacterial cellulose biosynthesis and in Glycan metabolism.

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

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome

Subcellular locationi

Topology

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

GO - Cellular componenti

Complete GO annotation...

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...

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.
OMAiIKQRERW.
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

        10         20         30         40         50
MPLVVPHAAM PEGRLMTAAS RRSASPLPTL ATWALWLLGA LLLVFVVAVP
60 70 80 90 100
MDVTQQLVFS GVLFAVALAV RNRGGRVVIL MMMGMSLAVS CRYIWWRMTQ
110 120 130 140 150
TMGVGSAVDF ILGLGLLGAE LYAFVILVLG YFQVLWPLNR KPVPLPADQR
160 170 180 190 200
LWPSVDVFIP TYNEPLSVVR TTVLAASVID WPAGKITIHL LDDGRRDEFR
210 220 230 240 250
AFCAEVGINY VTRTNNAHAK AGNINAALKK CSGDYVAIFD CDHIPTRSFL
260 270 280 290 300
QVAMGWFLHD TKLALVQMPH YFFSPDPFER NLDTHGKVPN EGELFYGLLQ
310 320 330 340 350
DGNDQWNATF FCGSCAVIKR TALEEVGGVA VETVTEDAHT ALKLQRRGYR
360 370 380 390 400
TAYLAVPQAA GLATESLSGH VAQRIRWARG MAQIARIDNP LLGRGLKLSQ
410 420 430 440 450
RLCYLNAMLH FFYGVPRIIY LTAPLAYLFF GAHVIQASAL MILAYALPHI
460 470 480 490 500
LQANLTNLRV QSRFRHLLWN EVYETTLAWY IFRPTLVALL NPKLGKFNVT
510 520 530 540 550
PKGGLVARSY FDAQIAKPYL FLLLLNVVGM VAGVLRLIYV GGSGEQQTIW
560 570 580 590 600
FNLAWTLYNM VLLGATIATA SETRQVRSAH RVPLDVPVTL YLPDGDVLPS
610 620 630 640 650
RSVNFSTGGM AIMLAQPQPI EPGLPVQIGL SHRGVEQTLP AVVRQDRDGQ
660 670 680 690 700
VSIQFTQMSM EQERWLVAST FARADIWLSQ WGQHDRDAFW RSMGQVLEAS
710 720
ARGFGRLGGH IVDSARQGFR PRRAVDLES
Length:729
Mass (Da):80,915
Last modified:July 26, 2002 - v1
Checksum:iB9C08BB995E795B1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008923 Genomic DNA. Translation: AAM38361.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008923 Genomic DNA. Translation: AAM38361.1.

3D structure databases

ProteinModelPortaliP58932.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi190486.XAC3518.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiCOG1215.
HOGENOMiHOG000259144.
KOiK00694.
OMAiIKQRERW.
OrthoDBiEOG66TG3C.

Enzyme and pathway databases

UniPathwayiUPA00694.
BioCyciXAXO190486:GH55-3518-MONOMER.

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.
ProtoNetiSearch...

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: April 29, 2015
This is version 89 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.