ID BCSQP_ECOLI Reviewed; 242 AA. AC P37655; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2017, sequence version 4. DT 04-NOV-2026, entry version 140. DE RecName: Full=Putative cellulose biosynthesis protein BcsQ; GN Name=bcsQ; Synonyms=yhjQ; OrderedLocusNames=b3534; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; 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]. 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 IDENTIFICATION OF MUTATION THAT GENERATES PSEUDOGENE, AND RESTORATION OF RP THE READING FRAME AND CELLULOSE PRODUCTION. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; 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: A C-terminal pseudogene fragment of BcsQ, which has a CC premature stop codon at position 6 of the intact protein. The mutation CC prevents cellulose synthesis, and has polar effects on transcription of CC downstream gene bcsA and probably also bcsB, bcsZ and bcsC CC (PubMed:24097954). When the reading frame is restored cellulose CC biosynthesis is also restored, see (AC P0DP92) for an intact protein. CC May play a role in subcellular localization of an active cellulose CC biosynthesis apparatus at the bacterial cell pole (By similarity). CC {ECO:0000250|UniProtKB:P0DP92, ECO:0000305|PubMed:24097954}. CC -!- INDUCTION: Part of the yhjR-bcsQABZC operon (PubMed:24097954). CC {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 this gene. The sequence CC given here starts on a GTG codon 6 nucleotides downstream of the CC premature stop codon. {ECO:0000269|PubMed:24097954}. CC -!- SIMILARITY: Belongs to the BcsQ family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. The protein is missing 8 CC N-terminal amino acids due to a premature stop codon; when the reading CC frame is restored strain W3110 synthesizes cellulose. See (AC P0DP92) CC for a functional intact protein. {ECO:0000305|PubMed:24097954}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U00039; AAB18512.1; -; Genomic_DNA. DR EMBL; U00096; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; S47756; S47756. DR RefSeq; WP_011310329.1; NZ_CP009789.1. DR AlphaFoldDB; P37655; -. DR SMR; P37655; -. DR DIP; DIP-12388N; -. DR FunCoup; P37655; 51. DR IntAct; P37655; 2. DR jPOST; P37655; -. DR KEGG; ecoc:C3026_19145; -. DR EchoBASE; EB2170; -. DR InParanoid; P37655; -. DR OrthoDB; 5288747at2; -. DR PhylomeDB; P37655; -. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IBA:GO_Central. DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central. DR FunFam; 3.40.50.300:FF:000943; Cellulose synthase operon protein YhjQ; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR017746; Cellulose_synthase_operon_BcsQ. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR050625; ParA/MinD_ATPase. DR NCBIfam; NF007460; bcsQ; 1. DR NCBIfam; TIGR03371; cellulose_yhjQ; 1. DR PANTHER; PTHR43384:SF4; CELLULOSE BIOSYNTHESIS PROTEIN BCSQ-RELATED; 1. DR PANTHER; PTHR43384; SEPTUM SITE-DETERMINING PROTEIN MIND HOMOLOG, CHLOROPLASTIC-RELATED; 1. DR Pfam; PF06564; CBP_BcsQ; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. PE 5: Uncertain; KW ATP-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1..242 FT /note="Putative cellulose biosynthesis protein BcsQ" FT /id="PRO_0000169575" FT BINDING 1..8 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" SQ SEQUENCE 242 AA; 27140 MW; C4DD72EC40E124A9 CRC64; MRGGVGTTTI TAALAWSLQM LGENVLVVDA CPDNLLRLSF NVDFTHRQGW ARAMLDGQDW RDAGLRYTSQ LDLLPFGQLS IEEQENPQHW QTRLSDICSG LQQLKASGRY QWILIDLPRD ASQITHQLLS LCDHSLAIVN VDANCHIRLH QQALPDGAHI LINDFRIGSQ VQDDIYQLWL QSQRRLLPML IHRDEAMAEC LAAKQPVGEY RSDALAAEEI LTLANWCLLN YSGLKTPVGS AS //