BCSA_ECOLI
ID BCSA_ECOLI Reviewed; 872 AA.
AC P37653; P37654; P76712; P76713; Q2M7J5; Q8RSS7;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Cellulose synthase catalytic subunit [UDP-forming];
DE EC=2.4.1.12;
GN Name=bcsA; Synonyms=yhjO, yhjP; OrderedLocusNames=b3533, JW5665;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP CHARACTERIZATION.
RC STRAIN=ECOR 10, ECOR 12, and TOB1;
RX PubMed=11260463; DOI=10.1046/j.1365-2958.2001.02337.x;
RA Zogaj X., Nimtz M., Rohde M., Bokranz W., Roemling U.;
RT "The multicellular morphotypes of Salmonella typhimurium and Escherichia
RT coli produce cellulose as the second component of the extracellular
RT matrix.";
RL Mol. Microbiol. 39:1452-1463(2001).
RN [5]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / W3110 / AR3110;
RX PubMed=24097954; DOI=10.1128/jb.00946-13;
RA Serra D.O., Richter A.M., Hengge R.;
RT "Cellulose as an architectural element in spatially structured Escherichia
RT coli biofilms.";
RL J. Bacteriol. 195:5540-5554(2013).
CC -!- FUNCTION: Catalytic subunit of cellulose synthase. It polymerizes
CC uridine 5'-diphosphate glucose to cellulose, which is produced as an
CC extracellular component for mechanical and chemical protection at the
CC onset of the stationary phase, when the cells exhibit multicellular
CC behavior (rdar morphotype). Coexpression of cellulose and thin
CC aggregative fimbriae (curli fimbrae or fibers) leads to a hydrophobic
CC network with tightly packed cells embedded in a highly inert matrix
CC that confers cohesion, elasticity and tissue-like properties to
CC colonies (PubMed:24097954). {ECO:0000269|PubMed:11260463,
CC ECO:0000269|PubMed:24097954}.
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).
CC -!- PATHWAY: Glycan metabolism; bacterial cellulose biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- INDUCTION: Part of the yhjR-bcsQABZC operon. Expressed at low levels in
CC mid-log phase, expression increases as cells enter stationary phase,
CC the increase in stationary phase is dependent on rpoS
CC (PubMed:24097954). Expression is higher at 28 than 37 degrees Celsius
CC (at protein level) (PubMed:24097954). {ECO:0000269|PubMed:24097954}.
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 -!- DISRUPTION PHENOTYPE: When disrupted in a cellulose-synthesizing strain
CC (a strain K12 / W3110 derivative called AR3110 with a restored,
CC functional bcsQ gene), cellulose is no longer made and the rdar
CC morphotype is lost (PubMed:24097954). {ECO:0000269|PubMed:24097954}.
CC -!- MISCELLANEOUS: The genes bscA, bcsB, bcsZ and bcsC are constitutively
CC transcribed but cellulose synthesis occurs only when DgcC, a putative
CC transmembrane protein regulated by CsgD, is expressed. Cellulose
CC production is abolished in E.coli K12 / MG1655 and W3110 due to a
CC premature stop codon in bcsQ (PubMed:24097954).
CC {ECO:0000305|PubMed:24097954}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18510.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAB18511.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB18511.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U00039; AAB18510.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00039; AAB18511.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U00096; AAC76558.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77761.1; -; Genomic_DNA.
DR PIR; H65151; H65151.
DR PIR; S47754; S47754.
DR PIR; S47755; S47755.
DR RefSeq; NP_417990.4; NC_000913.3.
DR RefSeq; WP_000025892.1; NZ_SSZK01000039.1.
DR PDB; 7LBY; EM; 4.20 A; A=2-872.
DR PDBsum; 7LBY; -.
DR AlphaFoldDB; P37653; -.
DR SMR; P37653; -.
DR BioGRID; 4260855; 267.
DR BioGRID; 852361; 1.
DR DIP; DIP-12387N; -.
DR IntAct; P37653; 4.
DR STRING; 511145.b3533; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR TCDB; 4.D.3.1.6; the glycan glucosyl transferase (opgh) family.
DR PaxDb; P37653; -.
DR PRIDE; P37653; -.
DR EnsemblBacteria; AAC76558; AAC76558; b3533.
DR EnsemblBacteria; BAE77761; BAE77761; BAE77761.
DR GeneID; 948053; -.
DR KEGG; ecj:JW5665; -.
DR KEGG; eco:b3533; -.
DR PATRIC; fig|511145.12.peg.3644; -.
DR EchoBASE; EB2169; -.
DR eggNOG; COG1215; Bacteria.
DR HOGENOM; CLU_011907_5_0_6; -.
DR InParanoid; P37653; -.
DR OMA; QRLCYAN; -.
DR PhylomeDB; P37653; -.
DR BioCyc; EcoCyc:EG12260-MON; -.
DR BioCyc; MetaCyc:EG12260-MON; -.
DR UniPathway; UPA00694; -.
DR PRO; PR:P37653; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
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:0016758; F:hexosyltransferase activity; IBA:GO_Central.
DR GO; GO:0090540; P:bacterial cellulose biosynthetic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; c-di-GMP; Cell inner membrane; Cell membrane;
KW Cellulose biosynthesis; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..872
FT /note="Cellulose synthase catalytic subunit [UDP-forming]"
FT /id="PRO_0000059267"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 525..545
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 592..612
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 640..660
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 668..688
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 833..853
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 694..790
FT /note="PilZ"
FT REGION 271..364
FT /note="Catalytic subdomain A"
FT REGION 441..501
FT /note="Catalytic subdomain B"
FT ACT_SITE 313
FT /evidence="ECO:0000255"
FT ACT_SITE 457
FT /evidence="ECO:0000255"
FT BINDING 360
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000255"
SQ SEQUENCE 872 AA; 99785 MW; 14326B8A2EB228F7 CRC64;
MSILTRWLLI PPVNARLIGR YRDYRRHGAS AFSATLGCFW MILAWIFIPL EHPRWQRIRA
EHKNLYPHIN ASRPRPLDPV RYLIQTCWLL IGASRKETPK PRRRAFSGLQ NIRGRYHQWM
NELPERVSHK TQHLDEKKEL GHLSAGARRL ILGIIVTFSL ILALICVTQP FNPLAQFIFL
MLLWGVALIV RRMPGRFSAL MLIVLSLTVS CRYIWWRYTS TLNWDDPVSL VCGLILLFAE
TYAWIVLVLG YFQVVWPLNR QPVPLPKDMS LWPSVDIFVP TYNEDLNVVK NTIYASLGID
WPKDKLNIWI LDDGGREEFR QFAQNVGVKY IARTTHEHAK AGNINNALKY AKGEFVSIFD
CDHVPTRSFL QMTMGWFLKE KQLAMMQTPH HFFSPDPFER NLGRFRKTPN EGTLFYGLVQ
DGNDMWDATF FCGSCAVIRR KPLDEIGGIA VETVTEDAHT SLRLHRRGYT SAYMRIPQAA
GLATESLSAH IGQRIRWARG MVQIFRLDNP LTGKGLKFAQ RLCYVNAMFH FLSGIPRLIF
LTAPLAFLLL HAYIIYAPAL MIALFVLPHM IHASLTNSKI QGKYRHSFWS EIYETVLAWY
IAPPTLVALI NPHKGKFNVT AKGGLVEEEY VDWVISRPYI FLVLLNLVGV AVGIWRYFYG
PPTEMLTVVV SMVWVFYNLI VLGGAVAVSV ESKQVRRSHR VEMTMPAAIA REDGHLFSCT
VQDFSDGGLG IKINGQAQIL EGQKVNLLLK RGQQEYVFPT QVARVMGNEV GLKLMPLTTQ
QHIDFVQCTF ARADTWALWQ DSYPEDKPLE SLLDILKLGF RGYRHLAEFA PSSVKGIFRV
LTSLVSWVVS FIPRRPERSE TAQPSDQALA QQ
