BCSQ_ECOLI
ID BCSQ_ECOLI Reviewed; 250 AA.
AC P0DP92;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2017, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=Cellulose biosynthesis protein BcsQ;
GN Name=bcsQ {ECO:0000303|PubMed:19400787}; Synonyms=yhjQ;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, DOMAIN,
RP DISRUPTION PHENOTYPE, GENE NAME, AND MUTAGENESIS OF GLY-14; THR-15;
RP 220-SER--SER-250 AND 237-LEU--SER-250.
RC STRAIN=1094;
RX PubMed=19400787; DOI=10.1111/j.1365-2958.2009.06678.x;
RA Le Quere B., Ghigo J.M.;
RT "BcsQ is an essential component of the Escherichia coli cellulose
RT biosynthesis apparatus that localizes at the bacterial cell pole.";
RL Mol. Microbiol. 72:724-740(2009).
RN [2]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND RESTORATION OF READING
RP FRAME.
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: Essential for cellulose biosynthesis, shown for strain 1094,
CC a commensal, natural cellulose producer (PubMed:19400787). Also shown
CC in strain W3110 which has a restored reading frame (TAG stop codon to
CC TTG for amino acid 6, called strain AR3110) (PubMed:24097954, this
CC protein). May play a role in subcellular localization of an active
CC cellulose biosynthesis apparatus at the bacterial cell pole
CC (PubMed:19400787). The combination of cellulose and the curli fiber
CC network confer cohesion, elasticity and tissue-like properties to
CC colonies (PubMed:24097954). {ECO:0000269|PubMed:19400787,
CC ECO:0000269|PubMed:24097954}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19400787}.
CC Note=Localizes at the cell pole, this does not require any genes of the
CC divergently expressed yhjRbcsQABZC and bcsEFG operons.
CC {ECO:0000269|PubMed:19400787}.
CC -!- INDUCTION: Part of the yhjR-bcsQABZC operon (PubMed:19400787,
CC PubMed:24097954). Expressed at low levels in mid-log phase, expression
CC increases as cells enter stationary phase, the increase in stationary
CC phase is dependent on rpoS (PubMed:24097954). In K12 strains the
CC premature stop codon in position 8 has polar effects on downstream
CC genes, decreasing their expression about 10-fold (PubMed:24097954).
CC {ECO:0000269|PubMed:19400787, ECO:0000269|PubMed:24097954}.
CC -!- DOMAIN: The N-terminal putative ATP-binding domain is required for
CC function. The C-terminal region contributes to both localization and
CC function in cellulose synthesis. {ECO:0000269|PubMed:19400787}.
CC -!- DISRUPTION PHENOTYPE: Deletion abolishes cellulose production.
CC {ECO:0000269|PubMed:19400787, ECO:0000269|PubMed:24097954}.
CC -!- MISCELLANEOUS: Cellulose production is abolished in E.coli K12 / MG1655
CC and W3110 due to a premature stop codon in bcsQ. The C-terminal
CC pseudogene prediction is found here (AC P37655) (PubMed:24097954).
CC {ECO:0000269|PubMed:24097954}.
CC -!- SIMILARITY: Belongs to the BcsQ family. {ECO:0000305}.
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DR PDB; 6YAR; X-ray; 1.90 A; A/B=1-250.
DR PDB; 6YAY; X-ray; 2.09 A; A/B=1-250.
DR PDB; 6YB3; X-ray; 1.59 A; A/B=1-250.
DR PDB; 6YB5; X-ray; 1.59 A; A/B/H=1-250.
DR PDB; 6YBB; X-ray; 2.90 A; A/B=1-250.
DR PDB; 6YBU; X-ray; 2.49 A; A/B/G/H=1-250.
DR PDBsum; 6YAR; -.
DR PDBsum; 6YAY; -.
DR PDBsum; 6YB3; -.
DR PDBsum; 6YB5; -.
DR PDBsum; 6YBB; -.
DR PDBsum; 6YBU; -.
DR AlphaFoldDB; P0DP92; -.
DR SMR; P0DP92; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR017746; Cellulose_synthase_operon_BcsQ.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF06564; CBP_BcsQ; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03371; cellulose_yhjQ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Nucleotide-binding.
FT CHAIN 1..250
FT /note="Cellulose biosynthesis protein BcsQ"
FT /id="PRO_0000441757"
FT BINDING 9..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VARIANT 249
FT /note="A -> K (in strain: 1094)"
FT MUTAGEN 14
FT /note="G->S: Loss of cellulose production, still localizes
FT to the cell pole."
FT /evidence="ECO:0000269|PubMed:19400787"
FT MUTAGEN 15
FT /note="T->Q: Does not alter cellulose production."
FT /evidence="ECO:0000269|PubMed:19400787"
FT MUTAGEN 220..250
FT /note="Missing: No cellulose production, 23% of protein
FT localizes to the cell pole."
FT /evidence="ECO:0000269|PubMed:19400787"
FT MUTAGEN 237..250
FT /note="Missing: Produces cellulose, 44% of protein
FT localizes to the cell pole."
FT /evidence="ECO:0000269|PubMed:19400787"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:6YB3"
FT HELIX 15..28
FT /evidence="ECO:0007829|PDB:6YB3"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:6YB3"
FT HELIX 44..48
FT /evidence="ECO:0007829|PDB:6YB3"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:6YB3"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:6YB3"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:6YB3"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:6YB3"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:6YB3"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:6YB3"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:6YB3"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:6YB3"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:6YB3"
FT STRAND 141..150
FT /evidence="ECO:0007829|PDB:6YB3"
FT HELIX 151..156
FT /evidence="ECO:0007829|PDB:6YB3"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:6YB3"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:6YB3"
FT HELIX 178..190
FT /evidence="ECO:0007829|PDB:6YB3"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:6YBU"
FT HELIX 203..210
FT /evidence="ECO:0007829|PDB:6YB3"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:6YB3"
FT HELIX 223..238
FT /evidence="ECO:0007829|PDB:6YB3"
SQ SEQUENCE 250 AA; 27878 MW; E0A13C105B2D7AF7 CRC64;
MAVLGLQGVR GGVGTTTITA ALAWSLQMLG ENVLVVDACP DNLLRLSFNV DFTHRQGWAR
AMLDGQDWRD AGLRYTSQLD LLPFGQLSIE EQENPQHWQT RLSDICSGLQ QLKASGRYQW
ILIDLPRDAS QITHQLLSLC DHSLAIVNVD ANCHIRLHQQ ALPDGAHILI NDFRIGSQVQ
DDIYQLWLQS QRRLLPMLIH RDEAMAECLA AKQPVGEYRS DALAAEEILT LANWCLLNYS
GLKTPVGSAS
