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Protein

Cellulose synthase catalytic subunit [UDP-forming]

Gene

bcsA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 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.

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).

Pathwayi: 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 sitei313 – 3131Sequence analysis
Binding sitei360 – 3601SubstrateSequence analysis
Binding sitei362 – 3621SubstrateSequence analysis
Active sitei457 – 4571Sequence analysis

GO - Molecular functioni

GO - Biological processi

  • bacterial cellulose biosynthetic process Source: EcoCyc
  • UDP-glucose metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Cellulose biosynthesis

Keywords - Ligandi

c-di-GMP

Enzyme and pathway databases

BioCyciEcoCyc:EG12260-MONOMER.
ECOL316407:JW5665-MONOMER.
UniPathwayiUPA00694.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.
TCDBi4.D.3.1.6. the glycan glucosyl transferase (opgh) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Cellulose synthase catalytic subunit [UDP-forming] (EC:2.4.1.12)
Gene namesi
Name:bcsA
Synonyms:yhjO, yhjP
Ordered Locus Names:b3533, JW5665
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12260. bcsA.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei30 – 5021HelicalSequence analysisAdd
BLAST
Transmembranei151 – 17121HelicalSequence analysisAdd
BLAST
Transmembranei173 – 19321HelicalSequence analysisAdd
BLAST
Transmembranei230 – 25021HelicalSequence analysisAdd
BLAST
Transmembranei525 – 54521HelicalSequence analysisAdd
BLAST
Transmembranei547 – 56721HelicalSequence analysisAdd
BLAST
Transmembranei592 – 61221HelicalSequence analysisAdd
BLAST
Transmembranei640 – 66021HelicalSequence analysisAdd
BLAST
Transmembranei668 – 68821HelicalSequence analysisAdd
BLAST
Transmembranei833 – 85321HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 872872Cellulose synthase catalytic subunit [UDP-forming]PRO_0000059267Add
BLAST

Proteomic databases

PaxDbiP37653.
PRIDEiP37653.

Interactioni

Protein-protein interaction databases

BioGridi4260855. 262 interactions.
DIPiDIP-12387N.
IntActiP37653. 3 interactions.
STRINGi511145.b3533.

Structurei

3D structure databases

ProteinModelPortaliP37653.
SMRiP37653. Positions 170-729.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini694 – 79097PilZAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni271 – 36494Catalytic subdomain AAdd
BLAST
Regioni441 – 50161Catalytic 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

eggNOGiENOG4107QZ7. Bacteria.
COG1215. LUCA.
HOGENOMiHOG000259144.
InParanoidiP37653.
KOiK00694.
OMAiQLTMGWF.
OrthoDBiEOG66TG3C.
PhylomeDBiP37653.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR003919. Cell_synth_A.
IPR005150. Cellulose_synth.
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR009875. PilZ_domain.
[Graphical view]
PfamiPF03552. Cellulose_synt. 1 hit.
PF00535. Glycos_transf_2. 1 hit.
PF07238. PilZ. 1 hit.
[Graphical view]
PRINTSiPR01439. CELLSNTHASEA.
SUPFAMiSSF53448. SSF53448. 1 hit.
TIGRFAMsiTIGR03030. CelA. 1 hit.

Sequencei

Sequence statusi: Complete.

P37653-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSILTRWLLI PPVNARLIGR YRDYRRHGAS AFSATLGCFW MILAWIFIPL
60 70 80 90 100
EHPRWQRIRA EHKNLYPHIN ASRPRPLDPV RYLIQTCWLL IGASRKETPK
110 120 130 140 150
PRRRAFSGLQ NIRGRYHQWM NELPERVSHK TQHLDEKKEL GHLSAGARRL
160 170 180 190 200
ILGIIVTFSL ILALICVTQP FNPLAQFIFL MLLWGVALIV RRMPGRFSAL
210 220 230 240 250
MLIVLSLTVS CRYIWWRYTS TLNWDDPVSL VCGLILLFAE TYAWIVLVLG
260 270 280 290 300
YFQVVWPLNR QPVPLPKDMS LWPSVDIFVP TYNEDLNVVK NTIYASLGID
310 320 330 340 350
WPKDKLNIWI LDDGGREEFR QFAQNVGVKY IARTTHEHAK AGNINNALKY
360 370 380 390 400
AKGEFVSIFD CDHVPTRSFL QMTMGWFLKE KQLAMMQTPH HFFSPDPFER
410 420 430 440 450
NLGRFRKTPN EGTLFYGLVQ DGNDMWDATF FCGSCAVIRR KPLDEIGGIA
460 470 480 490 500
VETVTEDAHT SLRLHRRGYT SAYMRIPQAA GLATESLSAH IGQRIRWARG
510 520 530 540 550
MVQIFRLDNP LTGKGLKFAQ RLCYVNAMFH FLSGIPRLIF LTAPLAFLLL
560 570 580 590 600
HAYIIYAPAL MIALFVLPHM IHASLTNSKI QGKYRHSFWS EIYETVLAWY
610 620 630 640 650
IAPPTLVALI NPHKGKFNVT AKGGLVEEEY VDWVISRPYI FLVLLNLVGV
660 670 680 690 700
AVGIWRYFYG PPTEMLTVVV SMVWVFYNLI VLGGAVAVSV ESKQVRRSHR
710 720 730 740 750
VEMTMPAAIA REDGHLFSCT VQDFSDGGLG IKINGQAQIL EGQKVNLLLK
760 770 780 790 800
RGQQEYVFPT QVARVMGNEV GLKLMPLTTQ QHIDFVQCTF ARADTWALWQ
810 820 830 840 850
DSYPEDKPLE SLLDILKLGF RGYRHLAEFA PSSVKGIFRV LTSLVSWVVS
860 870
FIPRRPERSE TAQPSDQALA QQ
Length:872
Mass (Da):99,785
Last modified:July 26, 2002 - v3
Checksum:i14326B8A2EB228F7
GO

Sequence cautioni

The sequence AAB18511.1 differs from that shown. Reason: Frameshift at position 128. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00039 Genomic DNA. Translation: AAB18510.1. Frameshift.
U00039 Genomic DNA. Translation: AAB18511.1. Frameshift.
U00096 Genomic DNA. Translation: AAC76558.2.
AP009048 Genomic DNA. Translation: BAE77761.1.
PIRiH65151.
S47754.
S47755.
RefSeqiNP_417990.4. NC_000913.3.
WP_000025892.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76558; AAC76558; b3533.
BAE77761; BAE77761; BAE77761.
GeneIDi948053.
KEGGiecj:JW5665.
eco:b3533.
PATRICi32122532. VBIEscCol129921_3644.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00039 Genomic DNA. Translation: AAB18510.1. Frameshift.
U00039 Genomic DNA. Translation: AAB18511.1. Frameshift.
U00096 Genomic DNA. Translation: AAC76558.2.
AP009048 Genomic DNA. Translation: BAE77761.1.
PIRiH65151.
S47754.
S47755.
RefSeqiNP_417990.4. NC_000913.3.
WP_000025892.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP37653.
SMRiP37653. Positions 170-729.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260855. 262 interactions.
DIPiDIP-12387N.
IntActiP37653. 3 interactions.
STRINGi511145.b3533.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.
TCDBi4.D.3.1.6. the glycan glucosyl transferase (opgh) family.

Proteomic databases

PaxDbiP37653.
PRIDEiP37653.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76558; AAC76558; b3533.
BAE77761; BAE77761; BAE77761.
GeneIDi948053.
KEGGiecj:JW5665.
eco:b3533.
PATRICi32122532. VBIEscCol129921_3644.

Organism-specific databases

EchoBASEiEB2169.
EcoGeneiEG12260. bcsA.

Phylogenomic databases

eggNOGiENOG4107QZ7. Bacteria.
COG1215. LUCA.
HOGENOMiHOG000259144.
InParanoidiP37653.
KOiK00694.
OMAiQLTMGWF.
OrthoDBiEOG66TG3C.
PhylomeDBiP37653.

Enzyme and pathway databases

UniPathwayiUPA00694.
BioCyciEcoCyc:EG12260-MONOMER.
ECOL316407:JW5665-MONOMER.

Miscellaneous databases

PROiP37653.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR003919. Cell_synth_A.
IPR005150. Cellulose_synth.
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR009875. PilZ_domain.
[Graphical view]
PfamiPF03552. Cellulose_synt. 1 hit.
PF00535. Glycos_transf_2. 1 hit.
PF07238. PilZ. 1 hit.
[Graphical view]
PRINTSiPR01439. CELLSNTHASEA.
SUPFAMiSSF53448. SSF53448. 1 hit.
TIGRFAMsiTIGR03030. CelA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
    Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
    Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION.
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "The multicellular morphotypes of Salmonella typhimurium and Escherichia coli produce cellulose as the second component of the extracellular matrix."
    Zogaj X., Nimtz M., Rohde M., Bokranz W., Roemling U.
    Mol. Microbiol. 39:1452-1463(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: ECOR 10, ECOR 12 and TOB1.

Entry informationi

Entry nameiBCSA_ECOLI
AccessioniPrimary (citable) accession number: P37653
Secondary accession number(s): P37654
, P76712, P76713, Q2M7J5, Q8RSS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 26, 2002
Last modified: January 20, 2016
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The genes bscA, bcsB, bcsZ and bcsC are constitutively transcribed but cellulose synthesis occurs only when AdrA, a putative transmembrane protein regulated by AgfD, is expressed. Cellulose production is abolished in E.coli K12.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.