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Reviewed, UniProtKB/Swiss-Prot Q8X5L7 (BCSA_ECO57)

Last modified June 16, 2009. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Cellulose synthase catalytic subunit [UDP-forming]
    EC=2.4.1.12
Gene names
Name: bcsA
Ordered Locus Names: Z4948, ECs4413
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length872 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

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 at the onset of the stationary phase, when the cells exhibit multicellular behavior (rdar morphotype). Coexpression of cellulose and thin aggregative fimbriae leads to a hydrophobic network with tightly packed cells embedded in a highly inert matrix By similarity.

Catalytic activity

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

Cofactor

Magnesium By similarity.

Enzyme regulation

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

Pathway

Glycan metabolism; bacterial cellulose biosynthesis.

Subcellular location

Cell inner membrane; Multi-pass membrane protein Potential.

Domain

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 similarities

Belongs to the glycosyltransferase 2 family.

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Ontologies

Keywords
   Biological processCellulose biosynthesis
   Cellular componentCell inner membrane
Cell membrane
Membrane
   DomainTransmembrane
   Ligandc-di-GMP
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processUDP-glucose metabolic process

Inferred from electronic annotation. Source: InterPro

cellulose biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to plasma membrane

Inferred from electronic annotation. Source: InterPro

   Molecular functioncellulose synthase (UDP-forming) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 872872Cellulose synthase catalytic subunit [UDP-forming]
PRO_0000059268

Regions

Transmembrane30 – 5021 Potential
Transmembrane151 – 17121 Potential
Transmembrane173 – 19321 Potential
Transmembrane230 – 25021 Potential
Transmembrane525 – 54521 Potential
Transmembrane547 – 56721 Potential
Transmembrane592 – 61221 Potential
Transmembrane640 – 66021 Potential
Transmembrane668 – 68821 Potential
Transmembrane833 – 85321 Potential
Region271 – 36494Catalytic subdomain A
Region441 – 50161Catalytic subdomain B

Sites

Active site3131 Potential
Active site4571 Potential
Binding site3601Substrate Potential
Binding site3621Substrate Potential

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Sequences

Sequence LengthMass (Da)Tools
Q8X5L7-1 [UniParc].

Last modified July 26, 2002. Version 2.
Checksum: F3F1A24A2B713FBA

FASTA87299,710
        10         20         30         40         50         60 
MSILTRWLLI PPVNARLIGR YRDYRRHGAS AFSATLGCFW MILAWIFIPL EHPRWQRIRA 

        70         80         90        100        110        120 
EHKNLYPHIN ASRPRPLDPV RYLIQTCWLL IGASRKETPK PRRRAFSGLQ NIRGRYHQWM 

       130        140        150        160        170        180 
NELPERVSHK TQHLDEKKEL GHLSAGARRL ILGIIVTFSL ILALICVTQP FNPLAQFIFL 

       190        200        210        220        230        240 
MLLWGGALIV RRMPGRFSAL MLIVLSLTVS CRYIWWRYTS TLNWDDPVSL VCGLILLFAE 

       250        260        270        280        290        300 
TYAWIVLVLG YFQVVWPLNR QPVPLPKDMS LWPSVDIFVP TYNEDLNVVK NTIYASLGID 

       310        320        330        340        350        360 
WPKDKLNIWI LDDGGREEFR QFAQNVGVKY IARTTHEHAK AGNINNALKY AKGEFVSIFD 

       370        380        390        400        410        420 
CDHVPTRSFL QMTVGWFLKE KQLAMMQTPH HFFSPDPFER NLGRFRKTPN EGTLFYGLVQ 

       430        440        450        460        470        480 
DGNDMWDATF FCGSCAVIRR KPLDEIGGIA VETVTEDAHT SLRLHRRGYT SAYMRIPQAA 

       490        500        510        520        530        540 
GLATESLSAH IGQRIRWARG MVQIFRLDNP LTGKGLKFAQ RLCYVNAMFH FLSGIPRLIF 

       550        560        570        580        590        600 
LTAPLAFLLL HAYIIYAPAL MIALFVLPHM IHASLTNSKI QGKYRHSFWS EIYETVLAWY 

       610        620        630        640        650        660 
IAPPTLVALI NPHKGKFNVT AKGGLVEEEY VDWVISRPYI FLVLLNLVGV AVGIWRYFYG 

       670        680        690        700        710        720 
PPTEMLTVVV SMVWVFYNLI VLGGAVAVSV ESKQVRRSHR VEMTMPAAIA REDGHLFSCT 

       730        740        750        760        770        780 
VQDFSDGGLG IKINGQAQIL EGQKVNLLLK RGQQEYVFPT QVARVMGNEV GLKLMPLTTQ 

       790        800        810        820        830        840 
QHIDFVQCTF ARADTWALWQ DSYPEDKPLE SLLDILKLGF RGYRHLAEFA PSSVKGIFRV 

       850        860        870 
LTSLVSWVVS FIPRRPERSE TAQPSDQALA QQ

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References

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed: 11206551] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

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Cross-references

Sequence databases

AE005174 Genomic DNA. Translation: AAG58675.1. Different initiation.
BA000007 Genomic DNA. Translation: BAB37836.1. Different initiation.
PIRE91180.
G86026.
RefSeqNP_290113.2.
NP_312440.2.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID915726.
961086.
GenomeReviewsGene locus Z4948 in contig AE005174_GR.
Gene locus ECs4413 in contig BA000007_GR.
KEGGece:Z4948.
ecs:ECs4413.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8X5L7.

Enzyme and pathway databases

BioCycECOL83334:ECS4413-MON.

Family and domain databases

InterProIPR003919. Cell_synth_A.
IPR017480. Cellulose_synth_catalytic.
IPR001173. Glyco_trans_2.
IPR009875. PilZ.
[Graphical view]
PfamPF00535. Glycos_transf_2. 1 hit.
PF07238. PilZ. 1 hit.
[Graphical view]
PRINTSPR01439. CELLSNTHASEA.
TIGRFAMsTIGR03030. CelA. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameBCSA_ECO57
AccessionPrimary (citable) accession number: Q8X5L7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: July 26, 2002
Last modified: June 16, 2009
This is version 52 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents