P58932 (BCSA_XANAC) Reviewed, UniProtKB/Swiss-Prot

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:	XAC3518

Organism

Xanthomonas axonopodis pv. citri (strain 306) [Complete proteome] [HAMAP]

Taxonomic identifier

190486 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas › Xanthomonas citri group › Xanthomonas campestris pv. citri › Xanthomonas citri pv. citri

Protein attributes

Sequence length	729 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 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.

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 – 729	729	Cellulose synthase catalytic subunit [UDP-forming]		PRO_0000059272
Regions
	Transmembrane	30 – 50	21	Helical; Potential
	Transmembrane	110 – 130	21	Helical; Potential
	Transmembrane	171 – 191	21	Helical; Potential
	Transmembrane	405 – 425	21	Helical; Potential
	Transmembrane	427 – 447	21	Helical; Potential
	Transmembrane	520 – 540	21	Helical; Potential
	Transmembrane	549 – 569	21	Helical; Potential
	Transmembrane	610 – 630	21	Helical; Potential
	Domain	575 – 671	97	PilZ
	Region	151 – 244	94	Catalytic subdomain A
	Region	321 – 381	61	Catalytic subdomain B
Sites
	Active site	193	1	Potential
	Active site	337	1	Potential
	Binding site	240	1	Substrate Potential
	Binding site	242	1	Substrate Potential

Sequences

	Sequence		Length	Mass (Da)
	P58932 [UniParc]. Last modified July 26, 2002. Version 1. Checksum: B9C08BB995E795B1	FASTA	729	80,915
	10 20 30 40 50 60 MPLVVPHAAM PEGRLMTAAS RRSASPLPTL ATWALWLLGA LLLVFVVAVP MDVTQQLVFS 70 80 90 100 110 120 GVLFAVALAV RNRGGRVVIL MMMGMSLAVS CRYIWWRMTQ TMGVGSAVDF ILGLGLLGAE 130 140 150 160 170 180 LYAFVILVLG YFQVLWPLNR KPVPLPADQR LWPSVDVFIP TYNEPLSVVR TTVLAASVID 190 200 210 220 230 240 WPAGKITIHL LDDGRRDEFR AFCAEVGINY VTRTNNAHAK AGNINAALKK CSGDYVAIFD 250 260 270 280 290 300 CDHIPTRSFL QVAMGWFLHD TKLALVQMPH YFFSPDPFER NLDTHGKVPN EGELFYGLLQ 310 320 330 340 350 360 DGNDQWNATF FCGSCAVIKR TALEEVGGVA VETVTEDAHT ALKLQRRGYR TAYLAVPQAA 370 380 390 400 410 420 GLATESLSGH VAQRIRWARG MAQIARIDNP LLGRGLKLSQ RLCYLNAMLH FFYGVPRIIY 430 440 450 460 470 480 LTAPLAYLFF GAHVIQASAL MILAYALPHI LQANLTNLRV QSRFRHLLWN EVYETTLAWY 490 500 510 520 530 540 IFRPTLVALL NPKLGKFNVT PKGGLVARSY FDAQIAKPYL FLLLLNVVGM VAGVLRLIYV 550 560 570 580 590 600 GGSGEQQTIW FNLAWTLYNM VLLGATIATA SETRQVRSAH RVPLDVPVTL YLPDGDVLPS 610 620 630 640 650 660 RSVNFSTGGM AIMLAQPQPI EPGLPVQIGL SHRGVEQTLP AVVRQDRDGQ VSIQFTQMSM 670 680 690 700 710 720 EQERWLVAST FARADIWLSQ WGQHDRDAFW RSMGQVLEAS ARGFGRLGGH IVDSARQGFR PRRAVDLES

References

[1]

"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities." da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P. , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P. Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 306.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008923 Genomic DNA. Translation: AAM38361.1.
RefSeq	NP_643825.2. NC_003919.1.
3D structure databases
ProteinModelPortal	P58932.
ModBase	Search...
Protein-protein interaction databases
STRING	190486.XAC3518.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM38361; AAM38361; XAC3518.
GeneID	1157589.
KEGG	xac:XAC3518.
PATRIC	24059178. VBIXanAxo33670_3640.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1215.
HOGENOM	HOG000259144.
KO	K00694.
OMA	LYVLPHM.
Enzyme and pathway databases
UniPathway	UPA00694.
Family and domain databases
InterPro	IPR003919. Cell_synth_A. IPR009875. PilZ_domain. [Graphical view]
Pfam	PF07238. PilZ. 1 hit. [Graphical view]
PRINTS	PR01439. CELLSNTHASEA.
TIGRFAMs	TIGR03030. CelA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

BCSA_XANAC

Accession

Primary (citable) accession number: P58932

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 26, 2002
Last sequence update:	July 26, 2002
Last modified:	May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program