BDCA_ECOLI
ID BDCA_ECOLI Reviewed; 237 AA.
AC P39333; Q2M659;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Cyclic-di-GMP-binding biofilm dispersal mediator protein;
GN Name=bdcA; Synonyms=yjgI; OrderedLocusNames=b4249, JW4207;
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=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP C-TERMINUS.
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 FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, GENE NAME, AND MUTAGENESIS OF
RP GLU-50.
RC STRAIN=K12 / BW25113;
RX PubMed=21059164; DOI=10.1111/j.1462-2920.2010.02368.x;
RA Ma Q., Yang Z., Pu M., Peti W., Wood T.K.;
RT "Engineering a novel c-di-GMP-binding protein for biofilm dispersal.";
RL Environ. Microbiol. 13:631-642(2011).
CC -!- FUNCTION: Increases biofilm dispersal. Acts by binding directly to the
CC signaling molecule cyclic-di-GMP, which decreases the intracellular
CC concentration of cyclic-di-GMP and leads to biofilm dispersal. Also
CC controls other biofilm-related phenotypes such as cell motility, cell
CC size, cell aggregation and production of extracellular DNA and
CC extracellular polysaccharides (EPS). Does not act as a
CC phosphodiesterase. {ECO:0000269|PubMed:21059164}.
CC -!- INDUCTION: Expression is time dependent in biofilms and is controlled
CC by BdcR. {ECO:0000269|PubMed:21059164}.
CC -!- DISRUPTION PHENOTYPE: Mutant shows decreased biofilm dispersal.
CC Deletion increases the cyclic-di GMP concentration in the cell.
CC {ECO:0000269|PubMed:21059164}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; U14003; AAA97146.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U00096; AAC77206.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78247.1; -; Genomic_DNA.
DR PIR; D65237; D65237.
DR RefSeq; NP_418670.1; NC_000913.3.
DR RefSeq; WP_000500727.1; NZ_STEB01000013.1.
DR PDB; 5Z2L; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J/K/L=1-237.
DR PDBsum; 5Z2L; -.
DR AlphaFoldDB; P39333; -.
DR SMR; P39333; -.
DR BioGRID; 4259560; 12.
DR DIP; DIP-12604N; -.
DR IntAct; P39333; 2.
DR STRING; 511145.b4249; -.
DR PaxDb; P39333; -.
DR PRIDE; P39333; -.
DR EnsemblBacteria; AAC77206; AAC77206; b4249.
DR EnsemblBacteria; BAE78247; BAE78247; BAE78247.
DR GeneID; 948765; -.
DR KEGG; ecj:JW4207; -.
DR KEGG; eco:b4249; -.
DR PATRIC; fig|511145.12.peg.4380; -.
DR EchoBASE; EB2418; -.
DR eggNOG; COG1028; Bacteria.
DR HOGENOM; CLU_010194_1_3_6; -.
DR InParanoid; P39333; -.
DR OMA; VGTLGKQ; -.
DR PhylomeDB; P39333; -.
DR BioCyc; EcoCyc:G7880-MON; -.
DR PRO; PR:P39333; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0035438; F:cyclic-di-GMP binding; IDA:EcoCyc.
DR GO; GO:0070402; F:NADPH binding; IDA:EcoCyc.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0044010; P:single-species biofilm formation; IMP:EcoCyc.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; c-di-GMP; Reference proteome.
FT CHAIN 1..237
FT /note="Cyclic-di-GMP-binding biofilm dispersal mediator
FT protein"
FT /id="PRO_0000054839"
FT ACT_SITE 146
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 10..34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MUTAGEN 50
FT /note="E->Q,V: Shows higher affinity for cyclic-di-GMP,
FT increases swimming motility and biofilm dispersal. Biofilm
FT formation is almost completely removed."
FT /evidence="ECO:0000269|PubMed:21059164"
FT TURN 3..6
FT /evidence="ECO:0007829|PDB:5Z2L"
FT STRAND 8..13
FT /evidence="ECO:0007829|PDB:5Z2L"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:5Z2L"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:5Z2L"
FT HELIX 41..51
FT /evidence="ECO:0007829|PDB:5Z2L"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:5Z2L"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:5Z2L"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:5Z2L"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:5Z2L"
FT HELIX 96..106
FT /evidence="ECO:0007829|PDB:5Z2L"
FT HELIX 108..120
FT /evidence="ECO:0007829|PDB:5Z2L"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:5Z2L"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:5Z2L"
FT HELIX 144..164
FT /evidence="ECO:0007829|PDB:5Z2L"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:5Z2L"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:5Z2L"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:5Z2L"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:5Z2L"
FT HELIX 206..216
FT /evidence="ECO:0007829|PDB:5Z2L"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:5Z2L"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:5Z2L"
SQ SEQUENCE 237 AA; 24598 MW; A99A3F23CE0116C0 CRC64;
MGAFTGKTVL ILGGSRGIGA AIVRRFVTDG ANVRFTYAGS KDAAKRLAQE TGATAVFTDS
ADRDAVIDVV RKSGALDILV VNAGIGVFGE ALELNADDID RLFKINIHAP YHASVEAARQ
MPEGGRILII GSVNGDRMPV AGMAAYAASK SALQGMARGL ARDFGPRGIT INVVQPGPID
TDANPANGPM RDMLHSLMAI KRHGQPEEVA GMVAWLAGPE ASFVTGAMHT IDGAFGA
