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Q93IN2 (BCSA_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:STM3619
OrganismSalmonella typhimurium
Taxonomic identifier90371 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length874 AA.
Sequence statusComplete.
Protein existenceInferred 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.

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 874874Cellulose synthase catalytic subunit [UDP-forming]
PRO_0000059270

Regions

Transmembrane30 – 5021Helical; Potential
Transmembrane151 – 17121Helical; Potential
Transmembrane173 – 19321Helical; Potential
Transmembrane230 – 25021Helical; Potential
Transmembrane525 – 54521Helical; Potential
Transmembrane547 – 56721Helical; Potential
Transmembrane592 – 61221Helical; Potential
Transmembrane634 – 65421Helical; Potential
Transmembrane668 – 68821Helical; Potential
Transmembrane833 – 85321Helical; Potential
Domain694 – 79097PilZ
Region271 – 36494Catalytic subdomain A
Region441 – 50161Catalytic subdomain B

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q93IN2 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 4C9421B58606310A

FASTA874100,044
        10         20         30         40         50         60 
MSALSRWLLI PPVSARLSER YQGYRRHGAS PFSAALGCLW TILAWIVFPL EHPRWQRIRD 

        70         80         90        100        110        120 
GHKALYPHIN AARPRPLDPA RYLIQTLWLV MISSTKERHE PRWRSFARLK DVRGRYHQWM 

       130        140        150        160        170        180 
DTLPERVRQK TTHLEKEKEL GHLSNGARRF ILGVIVTFSL ILALICITQP FNPLSQFIFL 

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

       250        260        270        280        290        300 
TYAWIVLVLG YFQVVWPLNR QPVPLPKEMS QWPTVDIFVP TYNEDLNVVK NTIYASLGID 

       310        320        330        340        350        360 
WPKDKLNIWI LDDGGRESFR HFARHVGVHY IARTTHEHAK AGNINNALKH AKGEFVAIFD 

       370        380        390        400        410        420 
CDHVPTRSFL QMTMGWFLKE 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 LFGKGLKLAQ RLCYLNAMFH FLSGIPRLIF 

       550        560        570        580        590        600 
LTAPLAFLLL HAYIIYAPAL MIALFVIPHM VHASLTNSKI QGKYRHSFWS EIYETVLAWY 

       610        620        630        640        650        660 
IAPPTLVALI NPHKGKFNVT AKGGLVEEKY VDWVISRPYI FLVLLNLLGV AAGVWRYYYG 

       670        680        690        700        710        720 
PENETLTVIV SLVWVFYNLV ILGGAVAVSV ESKQVRRAHR VEIAMPGAIA REDGHLFSCT 

       730        740        750        760        770        780 
VHDFSDGGLG IKINGQAQVL EGQKVNLLLK RGQQEYVFPT QVVRVTGNEV GLQLMPLTTK 

       790        800        810        820        830        840 
QHIDFVQCTF ARADTWALWQ DSFPEDKPLE SLLDILKLGF RGYRHLAEFA PPSVKVIFRS 

       850        860        870 
LTALIAWIVS FIPRRPERQA AIQPSDRVMA QAQQ 

« Hide

References

« Hide 'large scale' references
[1]"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: 11260463] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 14028 / SGSG 2980 / CDC 6516-60 / NCTC 12023.
[2]"Genetic analysis of Salmonella enteritidis biofilm formation: critical role of cellulose."
Solano C., Garcia B., Valle J., Berasain C., Ghigo J.-M., Gamazo C., Lasa I.
Mol. Microbiol. 43:793-808(2002) [PubMed: 11929533] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: LT2.
[3]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed: 11677609] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ315770 Genomic DNA. Translation: CAC44015.1.
AE006468 Genomic DNA. Translation: AAL22479.1.
AJ315148 Genomic DNA. Translation: CAC86199.1.
RefSeqNP_462520.1. NC_003197.1.

3D structure databases

ProteinModelPortalQ93IN2.
ModBaseSearch...

Protein family/group databases

CAZyGT2. Glycosyltransferase Family 2.

Proteomic databases

PRIDEQ93IN2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1255142.
GenomeReviewsGene locus STM3619 in contig AE006468_GR.
KEGGstm:STM3619.
NMPDRfig|99287.1.peg.3496.
PATRIC32386055. VBISalEnt20916_3825.

Phylogenomic databases

HOGENOMHBG632848.
OMACYANAML.
ProtClustDBPRK11498.

Enzyme and pathway databases

BioCycSTYP99287:STM3619-MONOMER.

Family and domain databases

InterProIPR003919. Cell_synth_A.
IPR001173. Glyco_trans_2.
IPR009875. PilZ_domain.
[Graphical view]
KOK00694.
PfamPF00535. Glycos_transf_2. 1 hit.
PF07238. PilZ. 1 hit.
[Graphical view]
PRINTSPR01439. CELLSNTHASEA.
TIGRFAMsTIGR03030. CelA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBCSA_SALTY
AccessionPrimary (citable) accession number: Q93IN2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: December 1, 2001
Last modified: January 25, 2012
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families