Reviewed, UniProtKB/Swiss-Prot P21877 (ACSA1_ACEXY)

Names and origin

Protein names

Recommended name:
    Cellulose synthase 1
Including the following 2 domains:
    1- Recommended name:
            Cellulose synthase catalytic domain [UDP-forming]
              EC=2.4.1.12
    2- Recommended name:
            Cyclic di-GMP-binding domain
        Alternative name(s):
            Cellulose synthase 1 regulatory domain

Gene names

Name:	acsAB
Synonyms:	acsA, acsB

Organism

Acetobacter xylinus (Gluconacetobacter xylinus)

Taxonomic identifier

28448 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Gluconacetobacter

Protein attributes

Sequence length	1550 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Bifunctional protein comprised of a catalytic subunit and a regulatory subunit. The catalytic subunit of cellulose synthase 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. The regulatory subunit binds bis-(3'-5') cyclic diguanylic acid (c-di-GMP). Ref.5
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 c-di-GMP.
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	In the N-terminal section; belongs to the glycosyltransferase 2 family. In the C-terminal section; belongs to the acsB/bcsB family.
Caution	Was originally (Ref.1) proposed to encode for two separate adjacent ORFs, ascA and ascB.
Sequence caution	The sequence CAA38487.1 differs from that shown. Reason: Frameshift at position 678. The sequence CAA38488.1 differs from that shown. Reason: Frameshift at position 678.

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 – 1550	1550	Cellulose synthase 1		PRO_0000059260
Regions
	Transmembrane	26 – 46	21	Potential
	Transmembrane	47 – 67	21	Potential
	Transmembrane	106 – 126	21	Potential
	Transmembrane	398 – 418	21	Potential
	Transmembrane	423 – 443	21	Potential
	Transmembrane	468 – 488	21	Potential
	Transmembrane	507 – 527	21	Potential
	Transmembrane	547 – 567	21	Potential
	Transmembrane	1513 – 1533	21	Potential
	Region	1 – 741	741	Catalytic
	Region	147 – 240	94	Catalytic subdomain A
	Region	317 – 377	61	Catalytic subdomain B
	Region	742 – 1550	809	Cyclic di-GMP binding
Sites
	Active site	189	1	Potential
	Active site	333	1	Potential
	Binding site	236	1	Substrate Potential
	Binding site	238	1	Substrate Potential
Experimental info
	Mutagenesis	188	1	D → N: Decrease in activity. Ref.6
	Mutagenesis	188	1	D → P: Loss of activity. Ref.6
	Mutagenesis	189	1	D → Y: Loss of activity. Ref.6
	Mutagenesis	236	1	D → Y: Loss of activity. Ref.6
	Mutagenesis	333	1	D → R: Loss of activity. Ref.6
	Mutagenesis	369	1	Q → M: Loss of activity. Ref.6
	Mutagenesis	370	1	R → P: Loss of activity. Ref.6
	Mutagenesis	370	1	R → Q: Decrease in activity. Ref.6
	Mutagenesis	372	1	R → A: Loss of activity. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P21877-1 [UniParc]. Last modified July 26, 2002. Version 3. Checksum: 63AB8952BC39E961	FASTA	1,550	168,162
	10 20 30 40 50 60 MPEVRSSTQS ESGMSQWMGK ILSIRGAGLT IGVFGLCALI AATSVTLPPE QQLIVAFVCV 70 80 90 100 110 120 VIFFIVGHKP SRRSQIFLEV LSGLVSLRYL TWRLTETLSF DTWLQGLLGT MLLVAELYAL 130 140 150 160 170 180 MMLFLSYFQT IAPLHRAPLP LPPNPDEWPT VDIFVPTYNE ELSIVRLTVL GSLGIDWPPE 190 200 210 220 230 240 KVRVHILDDG RRPEFAAFAA ECGANYIARP TNEHAKAGNL NYAIGHTDGD YILIFDCDHV 250 260 270 280 290 300 PTRAFLQLTM GWMVEDPKIA LMQTPHHFYS PDPFQRNLSA GYRTPPEGNL FYGVVQDGND 310 320 330 340 350 360 FWDATFFCGS CAILRRTAIE QIGGFATQTV TEDAHTALKM QRLGWSTAYL RIPLAGGLAT 370 380 390 400 410 420 ERLILHIGQR VRWARGMLQI FRIDNPLFGR GLSWGQRLCY LSAMTSFLFA VPRVIFLSSP 430 440 450 460 470 480 LAFLFFGQNI IAASPLALLA YAIPHMFHAV GTASKINKGW RYSFWSEVYE TTMALFLVRV 490 500 510 520 530 540 TIVTLLSPSR GKFNVTDKGG LLEKGYFDLG AVYPNIILGL IMFGGLARGV YELSFGHLDQ 550 560 570 580 590 600 IAERAYLLNS AWAMLSLIII LAAIAVGRET QQKRNSHRIP ATIPVEVANA DGSIIVTGVT 610 620 630 640 650 660 EDLSMGGAAV KMSWPAKLSG PTPVYIRTVL DGEELILPAR IIRAGNGRGI FIWTIDNLQQ 670 680 690 700 710 720 EFSVIRLVFG RADAWVDWGN YKADRPLLSL MDMVLSVKGL FRSSGDIVHR SSPTKPLAGN 730 740 750 760 770 780 ALSDDTNNPS RKERVLKGTV KMVSLLALLT FASSAQAASA PRAVAAKAPA HQPEASDLPP 790 800 810 820 830 840 LPALLPATSG AAQAGAGDAG ANGPGSPTGQ PLAADSADAL VENAENTSDT ATVHNYTLKD 850 860 870 880 890 900 LGAAGSITMR GLAPLQGIEF GIPSDQLVTS ARLVLSGSMS PNLRPETNSV TMTLNEQYIG 910 920 930 940 950 960 TLRPDPAHPT FGPMSFEINP IFFVSGNRLN FNFASGSKGC SDITNDTLWA TISQNSQLQI 970 980 990 1000 1010 1020 TTIALPPRRL LSRLPQPFYD KNVRQHVTVP MVLAQTYDPQ ILKSAGILAS WFGKQTDFLG 1030 1040 1050 1060 1070 1080 VTFPVSSTIP QSGNAILIGV ADELPTSLGR PQVNGPAVLE LPNPSDANAT ILVVTGRDRD 1090 1100 1110 1120 1130 1140 EVITASKGIA FASAPLPTDS HMDVAPVDIA PRKPNDAPSF IAMDHPVRFG DLVTASKLQG 1150 1160 1170 1180 1190 1200 TGFTSGVLSV PFRIPPDLYT WRNRPYKMQV RFRSPAGEAK DVEKSRLDVG INEVYLHSYP 1210 1220 1230 1240 1250 1260 LRETHGLVGA VLQGVGLARP ASGMQVHDLD VPPWTVFGQD QLNFYFDAMP LARGICQSGA 1270 1280 1290 1300 1310 1320 ANNAFHLGLD PDSTIDFSRA HHIAQMPNLA YMATVGFPFT TYADLSQTAV VLPEHPNAAT 1330 1340 1350 1360 1370 1380 VGAYLDLMGF MGAATWYPVA GVDIVSADHV SDVADRNLLV ISTLATSGEI APLLSRSSYE 1390 1400 1410 1420 1430 1440 VADGHLRTVS HASALDNAIK AVDDPLTAFR DRDSKPQDVD TPLTGGVGAM IEAESPLTAG 1450 1460 1470 1480 1490 1500 RTVLALLSSD GAGLNNLLQM LGERKKQANI QGDLVVAHGE DLSSYRTSPV YTIGTLPLWL 1510 1520 1530 1540 1550 WPDWYMHNRP VRVLLVGLLG CILIVSVLAR ALARHATRRF KQLEDERRKS

References

[1]	"Cloning and sequencing of the cellulose synthase catalytic subunit gene of Acetobacter xylinum." Saxena I.M., Lin F.C., Brown R.M. Jr. Plant Mol. Biol. 15:673-683(1990) [PubMed: 2151718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 6-20. Strain: ATCC 53582.
[2]	"Identification of a new gene in an operon for cellulose biosynthesis in Acetobacter xylinum." Saxena I.M., Lin F.C., Brown R.M. Jr. Plant Mol. Biol. 16:947-954(1991) [PubMed: 1830823] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 768-781. Strain: ATCC 53582.
[3]	"Characterization of genes in the cellulose-synthesizing operon (acs operon) of Acetobacter xylinum: implications for cellulose crystallization." Saxena I.M., Kudlicka K., Okuda K., Brown R.M. Jr. J. Bacteriol. 176:5735-5752(1994) [PubMed: 8083166] [Abstract] Cited for: SEQUENCE REVISION. Strain: ATCC 53582.
[4]	"A new gene required for cellulose production and a gene encoding cellulolytic activity in Acetobacter xylinum are colocalized with the bcs operon." Standal R., Iversen T.-G., Coucheron D.H., Fjaervik E., Blatny J.M., Valla S. J. Bacteriol. 176:665-672(1994) [PubMed: 8300521] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8. Strain: ATCC 23769 / NCIB 8246.
[5]	"Identification of the uridine 5'-diphosphoglucose (UDP-Glc) binding subunit of cellulose synthase in Acetobacter xylinum using the photoaffinity probe 5-azido-UDP-Glc." Lin F.C., Brown R.M. Jr., Drake R.R. Jr., Haley B.E. J. Biol. Chem. 265:4782-4784(1990) [PubMed: 2138620] [Abstract] Cited for: FUNCTION. Strain: ATCC 53582.
[6]	"Structure-function characterization of cellulose synthase: relationship to other glycosyltransferases." Saxena I.M., Brown R.M. Jr., Dandekar T. Phytochemistry 57:1135-1148(2001) [PubMed: 11430986] [Abstract] Cited for: 3D-STRUCTURE MODELING, MUTAGENESIS OF ASP-188; ASP-189; ASP-236; ASP-333; GLN-369; ARG-370 AND ARG-372. Strain: ATCC 23769 / NCIB 8246.
[7]	"Multidomain architecture of beta-glycosyl transferases: implications for mechanism of action." Saxena I.M., Brown R.M. Jr., Fevre M., Geremia R.A., Henrissat B. J. Bacteriol. 177:1419-1424(1995) [PubMed: 7883697] [Abstract] Cited for: REVIEW ON DOMAIN ARCHITECTURE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X54676 Genomic DNA. Translation: CAA38487.1. Frameshift. X54676 Genomic DNA. Translation: CAA38488.1. Frameshift. M96060 Unassigned DNA. Translation: AAA16971.1.
PIR	C36963. S13732. S16266.
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GT2. Glycosyltransferase Family 2.
Family and domain databases
InterPro	IPR003920. Cell_synth_B. IPR018513. Cell_synthase_bac. IPR017480. Cellulose_synth_catalytic. IPR001173. Glyco_trans_2. IPR009875. PilZ. [Graphical view]
Pfam	PF03170. BcsB. 1 hit. PF00535. Glycos_transf_2. 1 hit. PF07238. PilZ. 1 hit. [Graphical view]
PRINTS	PR01440. CELLSNTHASEB.
TIGRFAMs	TIGR03030. CelA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ACSA1_ACEXY

Accession

Primary (citable) accession number: P21877
Secondary accession number(s): P37717

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	July 26, 2002
Last modified:	June 16, 2009
This is version 76 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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