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Protein

Cellulose synthase catalytic subunit [UDP-forming]

Gene

bcsA

Organism
Komagataeibacter xylinus (Gluconacetobacter xylinus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalytic subunit of cellulose synthase. It polymerizes uridine 5'-diphosphate glucose to cellulose. The thick cellulosic mats generated by this enzyme probably provide a specialized protective environment to the bacterium (By similarity).By similarity

Catalytic activityi

UDP-glucose + (1,4-beta-D-glucosyl)(n) = UDP + (1,4-beta-D-glucosyl)(n+1).

Cofactori

Mg2+By similarity

Enzyme regulationi

Activated by bis-(3'-5') cyclic diguanylic acid (c-di-GMP).

Pathwayi: bacterial cellulose biosynthesis

This protein is involved in the pathway bacterial cellulose biosynthesis, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway bacterial cellulose biosynthesis and in Glycan metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei189Sequence analysis1
Binding sitei238SubstrateSequence analysis1
Binding sitei240SubstrateSequence analysis1
Active sitei335Sequence analysis1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Cellulose biosynthesis

Keywords - Ligandi

c-di-GMP

Enzyme and pathway databases

UniPathwayiUPA00694.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.

Names & Taxonomyi

Protein namesi
Recommended name:
Cellulose synthase catalytic subunit [UDP-forming] (EC:2.4.1.12)
Gene namesi
Name:bcsA
OrganismiKomagataeibacter xylinus (Gluconacetobacter xylinus)
Taxonomic identifieri28448 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeKomagataeibacter

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei27 – 47HelicalSequence analysisAdd BLAST21
Transmembranei49 – 69HelicalSequence analysisAdd BLAST21
Transmembranei106 – 126HelicalSequence analysisAdd BLAST21
Transmembranei167 – 187HelicalSequence analysisAdd BLAST21
Transmembranei409 – 429HelicalSequence analysisAdd BLAST21
Transmembranei432 – 452HelicalSequence analysisAdd BLAST21
Transmembranei470 – 490HelicalSequence analysisAdd BLAST21
Transmembranei517 – 537HelicalSequence analysisAdd BLAST21
Transmembranei551 – 571HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000592631 – 756Cellulose synthase catalytic subunit [UDP-forming]Add BLAST756

Structurei

3D structure databases

ProteinModelPortaliO82859.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini576 – 681PilZAdd BLAST106

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni147 – 242Catalytic subdomain AAdd BLAST96
Regioni319 – 379Catalytic subdomain BAdd BLAST61

Domaini

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 similaritiesi

Belongs to the glycosyltransferase 2 family.Curated
Contains 1 PilZ domain.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR003919. Cell_synth_A.
IPR005150. Cellulose_synth.
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR009875. PilZ_domain.
[Graphical view]
PfamiPF03552. Cellulose_synt. 1 hit.
PF00535. Glycos_transf_2. 1 hit.
PF07238. PilZ. 1 hit.
[Graphical view]
PRINTSiPR01439. CELLSNTHASEA.
SUPFAMiSSF53448. SSF53448. 1 hit.
TIGRFAMsiTIGR03030. CelA. 1 hit.

Sequencei

Sequence statusi: Complete.

O82859-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEVQSPVPT ESRLGRISNK ILSLRGASYI VGALGLCALI AATTVTLNNN
60 70 80 90 100
EQLIVAAVCV VIFFVVGRGK SRRTQIFLEV LSALVSLRYL TWRLTETLDF
110 120 130 140 150
NTWIQGILGV ILLMAELYAL YMLFLSYFQT IQPLHRAPLP LPDNVDDWPT
160 170 180 190 200
VDIFIPTYDE QLSIVRLTVL GALGIDWPPD KVNVYILDDG VRPEFEQFAK
210 220 230 240 250
DCGALYIGRV DVDSAHAKAG NLNHAIKRTS GDYILILDCD HIPTRAFLQI
260 270 280 290 300
AMGWMVADRK IALMQTPHHF YSPDPFQRNL AVGYRTPPEG NLFYGVIQDG
310 320 330 340 350
NDFWDATFFC GSCAILRREA IESIGGFAVE TVTEDAHTAL RMQRRGWSTA
360 370 380 390 400
YLRIPVASGL ATERLTTHIG QRMRWARGMI QIFRVDNPML GRGLKLGQRL
410 420 430 440 450
CYLSAMTSFF FAIPRVIFLA SPLAFLFAGQ NIIAAAPLAV AAYALPHMFH
460 470 480 490 500
SIATAAKVNK GWRYSFWSEV YETTMALFLV RVTIVTLLFP SKGKFNVTEK
510 520 530 540 550
GGVLEEEEFD LGATYPNIIF ATIMMGGLLI GLFELIVRFN QLDVIARNAY
560 570 580 590 600
LLNCAWALIS LIILFAAIAV GRETKQVRYN HRVEAHIPVT VYDAPAEGQP
610 620 630 640 650
HTYYNATHGM TQDVSMGGVA VHIPLPDVTT GPVKKRIHAV LDGEEIDIPA
660 670 680 690 700
TMLRCTNGKA VFTWDNNDLD TERDIVRFVF GRADAWLQWN NYEDDRPLRS
710 720 730 740 750
LWSLLLSIKA LFRKKGKIMA NSRPKKKPLA LPVERREPTT IHSGQTQEGK

ISRAAS
Length:756
Mass (Da):84,562
Last modified:November 1, 1998 - v1
Checksum:i6954F39A25E73B0A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB010645 Genomic DNA. Translation: BAA31463.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB010645 Genomic DNA. Translation: BAA31463.1.

3D structure databases

ProteinModelPortaliO82859.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00694.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR003919. Cell_synth_A.
IPR005150. Cellulose_synth.
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR009875. PilZ_domain.
[Graphical view]
PfamiPF03552. Cellulose_synt. 1 hit.
PF00535. Glycos_transf_2. 1 hit.
PF07238. PilZ. 1 hit.
[Graphical view]
PRINTSiPR01439. CELLSNTHASEA.
SUPFAMiSSF53448. SSF53448. 1 hit.
TIGRFAMsiTIGR03030. CelA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiBCSA2_KOMXY
AccessioniPrimary (citable) accession number: O82859
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: November 1, 1998
Last modified: September 16, 2015
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.