BCSB_ECOLI
ID BCSB_ECOLI Reviewed; 779 AA.
AC P37652; P76711; Q2M7J4;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Cyclic di-GMP-binding protein;
DE AltName: Full=Cellulose synthase regulatory subunit;
DE Flags: Precursor;
GN Name=bcsB; Synonyms=yhjN; OrderedLocusNames=b3532, JW3500;
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].
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 TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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; Single-pass type I membrane
CC protein.
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.
CC -!- SIMILARITY: Belongs to the AcsB/BcsB family. {ECO:0000305}.
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DR EMBL; U00039; AAB18509.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76557.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77762.1; -; Genomic_DNA.
DR PIR; G65151; G65151.
DR RefSeq; NP_417989.1; NC_000913.3.
DR RefSeq; WP_001407405.1; NZ_LN832404.1.
DR PDB; 6YG8; EM; 3.00 A; A/B/C/D/E=1-779.
DR PDB; 7L2Z; EM; 3.40 A; A/B/C/D/E/F=26-779.
DR PDB; 7LBY; EM; 4.20 A; B=1-779.
DR PDBsum; 6YG8; -.
DR PDBsum; 7L2Z; -.
DR PDBsum; 7LBY; -.
DR AlphaFoldDB; P37652; -.
DR SMR; P37652; -.
DR BioGRID; 4262529; 271.
DR DIP; DIP-12386N; -.
DR IntAct; P37652; 4.
DR STRING; 511145.b3532; -.
DR TCDB; 4.D.3.1.6; the glycan glucosyl transferase (opgh) family.
DR PaxDb; P37652; -.
DR PRIDE; P37652; -.
DR EnsemblBacteria; AAC76557; AAC76557; b3532.
DR EnsemblBacteria; BAE77762; BAE77762; BAE77762.
DR GeneID; 948045; -.
DR KEGG; ecj:JW3500; -.
DR KEGG; eco:b3532; -.
DR PATRIC; fig|511145.12.peg.3643; -.
DR EchoBASE; EB2168; -.
DR eggNOG; COG1215; Bacteria.
DR HOGENOM; CLU_003556_1_1_6; -.
DR InParanoid; P37652; -.
DR OMA; FQYMNPM; -.
DR PhylomeDB; P37652; -.
DR BioCyc; EcoCyc:EG12259-MON; -.
DR BioCyc; MetaCyc:EG12259-MON; -.
DR UniPathway; UPA00694; -.
DR PRO; PR:P37652; -.
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: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 1: Evidence at protein level;
KW 3D-structure; c-di-GMP; Cell inner membrane; Cell membrane;
KW Cellulose biosynthesis; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..779
FT /note="Cyclic di-GMP-binding protein"
FT /id="PRO_0000000268"
FT TOPO_DOM 26..742
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 743..763
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 764..779
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:6YG8"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 106..119
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:7L2Z"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:6YG8"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:7L2Z"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:6YG8"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 166..174
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:6YG8"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:7L2Z"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:6YG8"
FT HELIX 241..257
FT /evidence="ECO:0007829|PDB:6YG8"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:6YG8"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 309..318
FT /evidence="ECO:0007829|PDB:6YG8"
FT HELIX 322..333
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 343..350
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:7L2Z"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:6YG8"
FT TURN 379..382
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:6YG8"
FT TURN 387..389
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 392..397
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 405..418
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 428..433
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 436..442
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 466..475
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 478..487
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 492..495
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 500..502
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 508..512
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 517..519
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 526..529
FT /evidence="ECO:0007829|PDB:6YG8"
FT HELIX 532..538
FT /evidence="ECO:0007829|PDB:6YG8"
FT HELIX 540..543
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 551..554
FT /evidence="ECO:0007829|PDB:6YG8"
FT HELIX 561..578
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 586..589
FT /evidence="ECO:0007829|PDB:6YG8"
FT TURN 591..596
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 599..605
FT /evidence="ECO:0007829|PDB:6YG8"
FT HELIX 609..612
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 614..616
FT /evidence="ECO:0007829|PDB:7L2Z"
FT STRAND 619..621
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 623..632
FT /evidence="ECO:0007829|PDB:6YG8"
FT TURN 644..646
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 647..659
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 662..669
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 672..684
FT /evidence="ECO:0007829|PDB:6YG8"
FT HELIX 685..695
FT /evidence="ECO:0007829|PDB:6YG8"
FT HELIX 698..701
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 706..711
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 716..718
FT /evidence="ECO:0007829|PDB:6YG8"
FT STRAND 725..728
FT /evidence="ECO:0007829|PDB:6YG8"
SQ SEQUENCE 779 AA; 86024 MW; F3188171DDC23918 CRC64;
MKRKLFWICA VAMGMSAFPS FMTQATPATQ PLINAEPAVA AQTEQNPQVG QVMPGVQGAD
APVVAQNGPS RDVKLTFAQI APPPGSMVLR GINPNGSIEF GMRSDEVVTK AMLNLEYTPS
PSLLPVQSQL KVYLNDELMG VLPVTKEQLG KKTLAQMPIN PLFISDFNRV RLEFVGHYQD
VCEKPASTTL WLDVGRSSGL DLTYQTLNVK NDLSHFPVPF FDPSDNRTNT 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 TITVMPKAPN EAQMETLLNT VGFIGAQTGF PAINLTVTDD GSTIQGKDAD
IMIIGGIPDK LKDDKQIDLL VQATESWVKT PMRQTPFPGI VPDESDRAAE TRSTLTSSGA
MAAVIGFQSP YNDQRSVIAL LADSPRGYEM LNDAVNDSGK RATMFGSVAV IRESGINSLR
VGDVYYVGHL PWFERVWYAL ANHPILLAVL AAISVILLAW VLWRLLRIIS RRRLNPDNE
