BCSE_ECOLI
ID BCSE_ECOLI Reviewed; 523 AA.
AC P37657; Q2M7J7;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Cyclic di-GMP binding protein BcsE {ECO:0000303|PubMed:24942809};
DE AltName: Full=Cellulose biosynthesis protein BcsE;
GN Name=bcsE; Synonyms=yhjS; OrderedLocusNames=b3536, JW3504;
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 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).
RN [5]
RP FUNCTION, C-DI-GMP-BINDING, DOMAIN, AND MUTAGENESIS OF ARG-139; ARG-287;
RP ARG-306; ARG-364; ARG-415 AND ASP-418.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=24942809; DOI=10.1111/mmi.12672;
RA Fang X., Ahmad I., Blanka A., Schottkowski M., Cimdins A., Galperin M.Y.,
RA Roemling U., Gomelsky M.;
RT "GIL, a new c-di-GMP-binding protein domain involved in regulation of
RT cellulose synthesis in enterobacteria.";
RL Mol. Microbiol. 93:439-452(2014).
CC -!- FUNCTION: Binds bis-(3'-5') cyclic diguanylic acid (c-di-GMP), the
CC ability to bind c-di-GMP is important for its function
CC (PubMed:24942809). {ECO:0000269|PubMed:24942809}.
CC -!- DOMAIN: The central domain (GIL, residues 153-492) is sufficient for c-
CC di-GMP binding. {ECO:0000269|PubMed:24942809}.
CC -!- DISRUPTION PHENOTYPE: When the bcsEFG operon is disrupted in a
CC cellulose-synthesizing strain (a strain K12 / W3110 derivative called
CC AR3110 with a restored, functional bcsQ gene), cellulose is no longer
CC made. {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 (PubMed:24097954).
CC {ECO:0000305|PubMed:24097954}.
CC -!- SIMILARITY: Belongs to the BcsE family. {ECO:0000305}.
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DR EMBL; U00039; AAB18514.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76561.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77759.1; -; Genomic_DNA.
DR PIR; S47758; S47758.
DR RefSeq; NP_417993.1; NC_000913.3.
DR RefSeq; WP_001204931.1; NZ_STEB01000018.1.
DR PDB; 6TJ0; X-ray; 2.20 A; A/B=217-523.
DR PDB; 6YBB; X-ray; 2.90 A; E/F=217-523.
DR PDB; 6YBU; X-ray; 2.49 A; E/F/K/L=349-523.
DR PDBsum; 6TJ0; -.
DR PDBsum; 6YBB; -.
DR PDBsum; 6YBU; -.
DR AlphaFoldDB; P37657; -.
DR SMR; P37657; -.
DR BioGRID; 4260852; 1.
DR DIP; DIP-12390N; -.
DR IntAct; P37657; 4.
DR STRING; 511145.b3536; -.
DR PaxDb; P37657; -.
DR PRIDE; P37657; -.
DR EnsemblBacteria; AAC76561; AAC76561; b3536.
DR EnsemblBacteria; BAE77759; BAE77759; BAE77759.
DR GeneID; 66672579; -.
DR GeneID; 948050; -.
DR KEGG; ecj:JW3504; -.
DR KEGG; eco:b3536; -.
DR PATRIC; fig|511145.12.peg.3647; -.
DR EchoBASE; EB2172; -.
DR eggNOG; ENOG502Z9EC; Bacteria.
DR HOGENOM; CLU_039389_2_0_6; -.
DR OMA; GCGANMV; -.
DR BioCyc; EcoCyc:EG12263-MON; -.
DR PRO; PR:P37657; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0035438; F:cyclic-di-GMP binding; IDA:EcoCyc.
DR GO; GO:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR017745; BcsE.
DR Pfam; PF10995; CBP_GIL; 1.
DR TIGRFAMs; TIGR03369; cellulose_bcsE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cellulose biosynthesis; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..523
FT /note="Cyclic di-GMP binding protein BcsE"
FT /id="PRO_0000169580"
FT REGION 153..492
FT /note="GIL domain, sufficient for c-di-GMP binding"
FT /evidence="ECO:0000269|PubMed:24942809"
FT MUTAGEN 139
FT /note="R->D: Wild-type c-di-GMP binding, complements a bcsE
FT deletion in S.typhimurium 14028."
FT /evidence="ECO:0000269|PubMed:24942809"
FT MUTAGEN 287
FT /note="R->D: Wild-type c-di-GMP binding."
FT /evidence="ECO:0000269|PubMed:24942809"
FT MUTAGEN 306
FT /note="R->D: Wild-type c-di-GMP binding."
FT /evidence="ECO:0000269|PubMed:24942809"
FT MUTAGEN 364
FT /note="R->D: Wild-type c-di-GMP binding."
FT /evidence="ECO:0000269|PubMed:24942809"
FT MUTAGEN 415
FT /note="R->D: No longer binds c-di-GMP, does not complement
FT a bcsE deletion in S.typhimurium 14028."
FT /evidence="ECO:0000269|PubMed:24942809"
FT MUTAGEN 418
FT /note="D->R: No longer binds c-di-GMP."
FT /evidence="ECO:0000269|PubMed:24942809"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:6YBB"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:6TJ0"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:6TJ0"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:6TJ0"
FT HELIX 251..258
FT /evidence="ECO:0007829|PDB:6TJ0"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:6TJ0"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:6TJ0"
FT HELIX 276..290
FT /evidence="ECO:0007829|PDB:6TJ0"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:6TJ0"
FT HELIX 307..316
FT /evidence="ECO:0007829|PDB:6TJ0"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:6TJ0"
FT HELIX 328..337
FT /evidence="ECO:0007829|PDB:6TJ0"
FT TURN 338..340
FT /evidence="ECO:0007829|PDB:6TJ0"
FT HELIX 351..355
FT /evidence="ECO:0007829|PDB:6TJ0"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:6TJ0"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:6YBU"
FT HELIX 369..381
FT /evidence="ECO:0007829|PDB:6TJ0"
FT STRAND 391..398
FT /evidence="ECO:0007829|PDB:6TJ0"
FT HELIX 404..410
FT /evidence="ECO:0007829|PDB:6TJ0"
FT STRAND 418..423
FT /evidence="ECO:0007829|PDB:6TJ0"
FT STRAND 426..432
FT /evidence="ECO:0007829|PDB:6TJ0"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:6TJ0"
FT HELIX 439..446
FT /evidence="ECO:0007829|PDB:6TJ0"
FT HELIX 451..454
FT /evidence="ECO:0007829|PDB:6TJ0"
FT STRAND 455..461
FT /evidence="ECO:0007829|PDB:6TJ0"
FT HELIX 464..474
FT /evidence="ECO:0007829|PDB:6TJ0"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:6TJ0"
FT HELIX 486..491
FT /evidence="ECO:0007829|PDB:6YBU"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:6YBU"
FT STRAND 502..507
FT /evidence="ECO:0007829|PDB:6YBU"
FT STRAND 510..512
FT /evidence="ECO:0007829|PDB:6YBB"
SQ SEQUENCE 523 AA; 59428 MW; 4241AF8CE7A9DC35 CRC64;
MRDIVDPVFS IGISSLWDEL RHMPAGGVWW FNVDRHEDAI SLANQTIASQ AETAHVAVIS
MDSDPAKIFQ LDDSQGPEKI KLFSMLNHEK GLYYLTRDLQ CSIDPHNYLF ILVCANNAWQ
NIPAERLRSW LDKMNKWSRL NHCSLLVINP GNNNDKQFSL LLEEYRSLFG LASLRFQGDQ
HLLDIAFWCN EKGVSARQQL SVQQQNGIWT LVQSEEAEIQ PRSDEKRILS NVAVLEGAPP
LSEHWQLFNN NEVLFNEART AQAATVVFSL QQNAQIEPLA RSIHTLRRQR GSAMKILVRE
NTASLRATDE RLLLACGANM VIPWNAPLSR CLTMIESVQG QKFSRYVPED ITTLLSMTQP
LKLRGFQKWD VFCNAVNNMM NNPLLPAHGK GVLVALRPVP GIRVEQALTL CRPNRTGDIM
TIGGNRLVLF LSFCRINDLD TALNHIFPLP TGDIFSNRMV WFEDDQISAE LVQMRLLAPE
QWGMPLPLTQ SSKPVINAEH DGRHWRRIPE PMRLLDDAVE RSS
