BCSA_PSEFS
ID BCSA_PSEFS Reviewed; 739 AA.
AC P58931; C3K5V4; Q8RSZ1;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Cellulose synthase catalytic subunit [UDP-forming];
DE EC=2.4.1.12;
GN Name=bcsA; Synonyms=wssB; OrderedLocusNames=PFLU_0301;
OS Pseudomonas fluorescens (strain SBW25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216595;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12019221; DOI=10.1093/genetics/161.1.33;
RA Spiers A.J., Kahn S.G., Bohannon J., Travisano M., Rainey P.B.;
RT "Adaptive divergence in experimental populations of Pseudomonas
RT fluorescens. I. Genetic and phenotypic bases of wrinkly spreader fitness.";
RL Genetics 161:33-46(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SBW25;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
CC -!- FUNCTION: Catalytic subunit of cellulose synthase. It polymerizes
CC uridine 5'-diphosphate glucose to cellulose, which is produced as an
CC extracellular component responsible for the structural integrity and
CC rigidity of self-supporting mats characteristic of the 'wrinkly
CC spreader' phenotype.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-
CC beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19929, Rhea:RHEA-
CC COMP:10033, Rhea:RHEA-COMP:10034, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18246, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.12;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by bis-(3'-5') cyclic diguanylic acid
CC (c-di-GMP). {ECO:0000250}.
CC -!- PATHWAY: Glycan metabolism; bacterial cellulose biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- DOMAIN: There are two conserved domains in the globular part of the
CC protein: the N-terminal domain (domain A) contains the conserved DXD
CC motif and is possibly involved in catalysis and substrate binding. The
CC C-terminal domain (domain B) contains the QXXRW motif and is present
CC only in processive glycosyl transferases. It could be involved in the
CC processivity function of the enzyme, possibly required for holding the
CC growing glycan chain in the active site.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; AY074776; AAL71842.1; -; Genomic_DNA.
DR EMBL; AM181176; CAY46578.1; -; Genomic_DNA.
DR RefSeq; WP_012721722.1; NC_012660.1.
DR AlphaFoldDB; P58931; -.
DR SMR; P58931; -.
DR STRING; 216595.PFLU_0301; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PRIDE; P58931; -.
DR EnsemblBacteria; CAY46578; CAY46578; PFLU_0301.
DR KEGG; pfs:PFLU_0301; -.
DR PATRIC; fig|216595.4.peg.534; -.
DR eggNOG; COG1215; Bacteria.
DR HOGENOM; CLU_011907_5_0_6; -.
DR OMA; QRLCYAN; -.
DR OrthoDB; 724641at2; -.
DR UniPathway; UPA00694; -.
DR Proteomes; UP000002332; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0035438; F:cyclic-di-GMP binding; IEA:InterPro.
DR GO; GO:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006011; P:UDP-glucose metabolic process; IEA:InterPro.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR003919; Cell_synth_A.
DR InterPro; IPR005150; Cellulose_synth.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR009875; PilZ_domain.
DR Pfam; PF03552; Cellulose_synt; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF07238; PilZ; 1.
DR PRINTS; PR01439; CELLSNTHASEA.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR03030; CelA; 1.
PE 3: Inferred from homology;
KW c-di-GMP; Cell inner membrane; Cell membrane; Cellulose biosynthesis;
KW Glycosyltransferase; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..739
FT /note="Cellulose synthase catalytic subunit [UDP-forming]"
FT /id="PRO_0000059271"
FT TRANSMEM 36..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..546
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 551..573
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 580..677
FT /note="PilZ"
FT REGION 157..250
FT /note="Catalytic subdomain A"
FT REGION 327..387
FT /note="Catalytic subdomain B"
FT ACT_SITE 199
FT /evidence="ECO:0000255"
FT ACT_SITE 343
FT /evidence="ECO:0000255"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT CONFLICT 415
FT /note="L -> Q (in Ref. 1; AAL71842)"
FT /evidence="ECO:0000305"
FT CONFLICT 644
FT /note="F -> K (in Ref. 1; AAL71842)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 739 AA; 82169 MW; BFA57F3987F3F982 CRC64;
MTDTTSSTPF VEGRAEQRLN GAIARFNRWP SAPRTVLVVA SCVLGAMLLL GIISAPLDLY
SQCLFAAVCF LAVLVLRKIP GRLAILALVV LSLVASLRYM FWRLTSTLGF ETWVDMFFGY
GLVAAEFYAL IVLIFGYVQT AWPLRRTPVW LKTEPEEWPT VDVFIPTYNE ALSIVKLTIF
AAQAMDWPKD KLRVHVLDDG RRDDFREFCR KVGVNYIRRD NNFHAKAGNL NEALKVTDGE
YIALFDADHV PTRSFLQVSL GWFLKDPKLA MLQTPHFFFS PDPFEKNLDT FRAVPNEGEL
FYGLVQDGND LWNATFFCGS CAVIRREPLL EIGGVAVETV TEDAHTALKL NRLGYNTAYL
AIPQAAGLAT ESLSRHINQR IRWARGMAQI FRTDNPLLGK GLKWGQRICY ANAMLHFFYG
LPRLVFLTAP LAYLIFGAEI FHASALMIVA YVLPHLVHSS LTNSRIQGRF RHSFWNEVYE
TVLAWYILPP VLVALVNPKA GGFNVTDKGG IIDKQFFDWK LARPYLVLLA VNLIGLGFGI
HQLIWGDAST AVTVAINLTW TLYNLIITSA AVAVASEARQ VRSEPRVSAK LPVSIICADG
RVLDGTTQDF SQNGFGLMLS DGHSITQGER VQLVLSRNGQ DSLFDARVVF SKGAQIGAQF
EALSLRQQSE LVRLTFSRAD TWAASWGAGQ PDTPLAALRE VGSIGIGGLF TLGRATLHEL
RLALSRTPTK PLDTLMDKP
