Reviewed, UniProtKB/Swiss-Prot P19449 (BCSA1_ACEXY)

Names and origin

Protein names

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

Gene names

Name:

bcsA

Organism

Acetobacter xylinus (Gluconacetobacter xylinus)

Taxonomic identifier

28448 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Gluconacetobacter

Protein attributes

Sequence length	754 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalytic subunit of cellulose synthase. It polymerizes uridine 5'-diphosphate glucose to cellulose in a processive way. The thick cellulosic mats generated by this enzyme probably provide a specialized protective environment to the bacterium.
Catalytic activity	UDP-glucose + (1,4-beta-D-glucosyl)(n) = UDP + (1,4-beta-D-glucosyl)(n+1).
Cofactor	Magnesium.
Enzyme regulation	Activated by bis-(3'-5') cyclic diguanylic acid (c-di-GMP). Ref.2
Pathway	Glycan metabolism; bacterial cellulose biosynthesis.
Subcellular location	Cell inner membrane; Multi-pass membrane protein Potential.
Induction	Cellulose is produced at a linear rate with respect to cell growth when O2 is present.
Domain	There are two conserved domains in the globular part of the catalytic subunit: 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.

Ontologies

Keywords
Biological process	Cellulose biosynthesis
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane
Ligand	c-di-GMP
Molecular function	Glycosyltransferase Transferase
Technical term	Direct protein sequencing
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 plasma membrane Inferred from electronic annotation. Source: InterPro
Molecular function	cellulose synthase (UDP-forming) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 754	754	Cellulose synthase catalytic subunit [UDP-forming]		PRO_0000059262
Regions
	Transmembrane	26 – 46	21	Potential
	Transmembrane	47 – 67	21	Potential
	Transmembrane	108 – 128	21	Potential
	Transmembrane	167 – 187	21	Potential
	Transmembrane	407 – 427	21	Potential
	Transmembrane	430 – 450	21	Potential
	Transmembrane	468 – 488	21	Potential
	Transmembrane	516 – 536	21	Potential
	Transmembrane	549 – 569	21	Potential
	Region	147 – 240	94	Catalytic subdomain A
	Region	317 – 377	61	Catalytic subdomain B
Sites
	Active site	189	1	Potential
	Active site	333	1	Potential
	Binding site	236	1	Substrate Potential
	Binding site	238	1	Substrate Potential

Sequences

	Sequence		Length	Mass (Da)
	P19449-1 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: 8D5FC1FE62E2C068	FASTA	754	84,443
	10 20 30 40 50 60 MSEVQSPVPA ESRLDRFSNK ILSLRGANYI VGALGLCALI AATTVTLSIN EQLIVALVCV 70 80 90 100 110 120 LVFFIVGRGK SRRTQIFLEV LSALVSLRYL TWRLTETLDF DTWIQGGLGV TLLMAELYAL 130 140 150 160 170 180 YMLFLSYFQT IQPLHRAPLP LPDNVDDWPT VDIFIPTYDE QLSIVRLTVL GALGIDWPPD 190 200 210 220 230 240 KVNVYILDDG VRPEFEQFAK DCGALYIGRV DSSHAKAGNL NHAIKRTSGD YILILDCDHI 250 260 270 280 290 300 PTRAFLQIAM GWMVADRKIA LMQTPHHFYS PDPFQRNLAV GYRTPPEGNL FYGVIQDGND 310 320 330 340 350 360 FWDATFFCGS CAILRREAIE SIGGFAVETV TEDAHTALRM QRRGWSTAYL RIPVASGLAT 370 380 390 400 410 420 ERLTTHIGQR MRWARGMIQI FRVDNPMLGG GLKLGQRLCY LSAMTSFFFA IPRVIFLASP 430 440 450 460 470 480 LAFLFFGQNI IAASPLAVLA YAIPHMFHSI ATAAKVNKGW RYSFWSEVYE TTMALFLVRV 490 500 510 520 530 540 TIITLMFPSK GKFNVTEKGG VLEEEEFDLG ATYPNIIFAG IMTLGLLIGL FELTFHFNQL 550 560 570 580 590 600 AGIAKRAYLL NCIWAMISLI ILLAAIAVGR ETKQVRYNHR VEAHIPVTVY EAPVAGQPNT 610 620 630 640 650 660 YHNATPGMTQ DVSMGGVAVH MPWPDVSTGP VKTRIHAVLD GEEIDIPATM LRCKNGKAVF 670 680 690 700 710 720 TWDNNDLDTE RDIVRFVFGR ADAWLQWNNY EDDRPLRSLW SLLLSIKALF RKKGKMMANS 730 740 750 RPKRKPLALP VERREPTTIQ SGQTQEGKIS RAAS

References

[1]

"Genetic organization of the cellulose synthase operon in Acetobacter xylinum." Wong H.C., Fear A.L., Calhoon R.D., Eichinger G.H., Mayer R., Amikam D., Benziman M., Gelfand D.H., Meade J.H., Emerick A.W., Bruner R., Ben-Bassat A., Tal R. Proc. Natl. Acad. Sci. U.S.A. 87:8130-8134(1990) [PubMed: 2146681] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-42 AND 196-206. Strain: 1306-3.

[2]

"Phosphodiesterase A1, a regulator of cellulose synthesis in Acetobacter xylinum, is a heme-based sensor." Chang A.L., Tuckerman J.R., Gonzalez G., Mayer R., Weinhouse H., Volman G., Amikam D., Benziman M., Gilles-Gonzalez M.-A. Biochemistry 40:3420-3426(2001) [PubMed: 11297407] [Abstract] Cited for: ENZYME REGULATION. Strain: 1306-3.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M37202 Genomic DNA. Translation: AAA21884.1.
PIR	A43735.
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GT2. Glycosyltransferase Family 2.
Family and domain databases
InterPro	IPR003919. Cell_synth_A. IPR017480. Cellulose_synth_catalytic. IPR001173. Glyco_trans_2. IPR009875. PilZ. [Graphical view]
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

BCSA1_ACEXY

Accession

Primary (citable) accession number: P19449

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)