BCSB_ECO57
ID BCSB_ECO57 Reviewed; 785 AA.
AC Q8X5L8;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Cyclic di-GMP-binding protein;
DE AltName: Full=Cellulose synthase regulatory subunit;
DE Flags: Precursor;
GN Name=bcsB; OrderedLocusNames=Z4947, ECs4412;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Binds the cellulose synthase activator, bis-(3'-5') cyclic
CC diguanylic acid (c-di-GMP). {ECO:0000250}.
CC -!- PATHWAY: Glycan metabolism; bacterial cellulose biosynthesis.
CC -!- SUBUNIT: Tightly associated with the cellulose synthase catalytic
CC subunit. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass
CC type I membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AcsB/BcsB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG58674.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG58674.2; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB37835.1; -; Genomic_DNA.
DR PIR; D91180; D91180.
DR PIR; F86026; F86026.
DR RefSeq; NP_312439.1; NC_002695.1.
DR RefSeq; WP_001302734.1; NZ_SDVX01000004.1.
DR AlphaFoldDB; Q8X5L8; -.
DR SMR; Q8X5L8; -.
DR STRING; 155864.EDL933_4787; -.
DR EnsemblBacteria; AAG58674; AAG58674; Z4947.
DR EnsemblBacteria; BAB37835; BAB37835; ECs_4412.
DR GeneID; 915722; -.
DR KEGG; ece:Z4947; -.
DR KEGG; ecs:ECs_4412; -.
DR PATRIC; fig|386585.9.peg.4613; -.
DR eggNOG; COG1215; Bacteria.
DR HOGENOM; CLU_003556_1_1_6; -.
DR UniPathway; UPA00694; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006011; P:UDP-glucose metabolic process; IEA:InterPro.
DR InterPro; IPR003920; Cell_synth_B.
DR InterPro; IPR018513; Cell_synthase_bac.
DR PANTHER; PTHR39083; PTHR39083; 1.
DR Pfam; PF03170; BcsB; 1.
DR PRINTS; PR01440; CELLSNTHASEB.
PE 3: Inferred from homology;
KW c-di-GMP; Cell inner membrane; Cell membrane; Cellulose biosynthesis;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..785
FT /note="Cyclic di-GMP-binding protein"
FT /id="PRO_0000000269"
FT TOPO_DOM 26..744
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 745..765
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 766..785
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 785 AA; 86675 MW; CE86E566C282E28D CRC64;
MKRKLFWICA VAMGMSAFPS FMTQATPATQ PLINAEPAVA AQTEQNPQVG QVMPGVQGAD
APVVAQNGPS RDVKLTFAQI APPPGSMVLR GINPNGSIEF GMRSDEVVTK AMLNLEYTPS
PSLLPVQSQL KVYLNDELMG VLPVTKEQLG KKTLAQMPIN PLFITDFNRV RLEFVGHYQD
VCENPASTTL WLDVGRSSGL DLTYQTLNVK NDLSHFPVPF FDPRDNRTNT LPMVFAGAPD
VGLQQASAIV ASWFGSRSGW RGQNFPVLYN QLPDRNAIVF ATNDKRPDFL RDHPAVKAPV
IEMINHPQNP YVKLLVVFGR DDKDLLQAAK GIAQGNILFR GESVVVNEVK PLLPRKPYDA
PNWVRTDRPV TFGELKTYEE QLQSSGLEPA AINVSLNLPP DLYLMRSTGI DMDINYRYTM
PPVKDSSRMD ISLNNQFLQS FNLSSKQEAN RLLLRIPVLQ GLLDGKTDVS IPALKLGATN
QLRFDFEYMN PMPGGSVDNC ITFQPVQNHV VIGDDSTIDF SKYYHFIPMP DLRAFANAGF
PFSRMADLSQ TITVMPKTPN EAQMETLLNT VGFIGAQTGF PAINLTVTDD GSTIQGKDAD
IMIIGGIPDK LKDDKQIDLL VQATESWVKT PMRQTPFPGI VPDESDRAAE TQSTLTSSGA
MAAVIGFQSP YNDQRSVIAL LADSPRGYEM LNDAVNDSGK RATMFGSVAV IRESGINSLR
VGDVYYVGHL PWFERLWYAL ANHPILLAVL AVLAVLAAIS VILLAWVLWR LLRIISRRRL
NPDNE