Cellulose synthase catalytic subunit [UDP-forming]

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Q8X5L7 (BCSA_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cellulose synthase catalytic subunit [UDP-forming]
EC=2.4.1.12

Gene names

Name:	bcsA
Ordered Locus Names:	Z4948, ECs4413

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	872 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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. Contains 1 PilZ domain.
Sequence caution	The sequence AAG58675.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAB37836.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Cellulose biosynthesis
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	c-di-GMP
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	UDP-glucose metabolic process Inferred from electronic annotation. Source: InterPro cellulose biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cellulose synthase (UDP-forming) activity Inferred from electronic annotation. Source: EC cyclic-di-GMP binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 872

872

Cellulose synthase catalytic subunit [UDP-forming]

PRO_0000059268

Regions

Transmembrane

30 – 50

Helical; Potential

Transmembrane

151 – 171

Helical; Potential

Transmembrane

173 – 193

Helical; Potential

Transmembrane

230 – 250

Helical; Potential

Transmembrane

525 – 545

Helical; Potential

Transmembrane

547 – 567

Helical; Potential

Transmembrane

592 – 612

Helical; Potential

Transmembrane

640 – 660

Helical; Potential

Transmembrane

668 – 688

Helical; Potential

Transmembrane

833 – 853

Helical; Potential

Domain

694 – 790

PilZ

Region

271 – 364

Catalytic subdomain A

Region

441 – 501

Catalytic subdomain B

Sites

Active site

313

Potential

Active site

457

Potential

Binding site

360

Substrate Potential

Binding site

362

Substrate Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q8X5L7 [UniParc].

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

FASTA

872

99,710

        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.

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.

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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG58675.1. Different initiation. BA000007 Genomic DNA. Translation: BAB37836.1. Different initiation.
PIR	E91180. G86026.
RefSeq	NP_290113.2. NC_002655.2. NP_312440.2. NC_002695.1.
3D structure databases
ProteinModelPortal	Q8X5L7.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000025921; EBESCP00000024814; EBESCG00000024974. EBESCT00000055804; EBESCP00000053632; EBESCG00000054852.
GeneID	915726. 961086.
GenomeReviews	Gene locus Z4948 in contig AE005174_GR. Gene locus ECs4413 in contig BA000007_GR.
KEGG	ece:Z4948. ecs:ECs4413.
PATRIC	18358409. VBIEscCol44059_4371.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000008881.
HOGENOM	HBG632848.
OMA	CYANAML.
ProtClustDB	PRK11498.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS4413-MONOMER.
Family and domain databases
InterPro	IPR003919. Cell_synth_A. IPR001173. Glyco_trans_2. IPR009875. PilZ_domain. [Graphical view]
KO	K00694.
Pfam	PF00535. Glycos_transf_2. 1 hit. PF07238. PilZ. 1 hit. [Graphical view]
PRINTS	PR01439. CELLSNTHASEA.
TIGRFAMs	TIGR03030. CelA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

BCSA_ECO57

Accession

Primary (citable) accession number: Q8X5L7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 26, 2002
Last sequence update:	July 26, 2002
Last modified:	January 25, 2012
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents