CSGD_ECOLI
ID CSGD_ECOLI Reviewed; 216 AA.
AC P52106;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=CsgBAC operon transcriptional regulatory protein;
GN Name=csgD; OrderedLocusNames=b1040, JW1023;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8817489; DOI=10.1111/j.1365-2958.1995.mmi_18040661.x.;
RA Hammar M., Arnqvist A., Bian Z., Olsen A., Normark S.;
RT "Expression of two csg operons is required for production of
RT fibronectin- and congo red-binding curli polymers in Escherichia coli K-
RT 12.";
RL Mol. Microbiol. 18:661-670(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-216.
RC STRAIN=O78;
RA Seijffers R., Gophna U., Ron E.Z.;
RT "Avian E. coli serotype O78 csg cluster.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, REGULATION TARGETS, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / PHL565;
RX PubMed=16513732; DOI=10.1128/jb.188.6.2027-2037.2006;
RA Brombacher E., Baratto A., Dorel C., Landini P.;
RT "Gene expression regulation by the Curli activator CsgD protein: modulation
RT of cellulose biosynthesis and control of negative determinants for
RT microbial adhesion.";
RL J. Bacteriol. 188:2027-2037(2006).
RN [7]
RP INDUCTION.
RC STRAIN=K12 / MC4100;
RX PubMed=17010156; DOI=10.1111/j.1365-2958.2006.05440.x;
RA Weber H., Pesavento C., Possling A., Tischendorf G., Hengge R.;
RT "Cyclic-di-GMP-mediated signalling within the sigma network of Escherichia
RT coli.";
RL Mol. Microbiol. 62:1014-1034(2006).
RN [8]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=24212724; DOI=10.1038/srep03186;
RA Soo V.W., Wood T.K.;
RT "Antitoxin MqsA represses curli formation through the master biofilm
RT regulator CsgD.";
RL Sci. Rep. 3:3186-3186(2013).
CC -!- FUNCTION: The master regulator for adhesive curli fimbriae expression;
CC necessary for transcription of the csgBAC/ymdA operon. Plays a positive
CC role in biofilm formation. May have the capability to respond to
CC starvation and/or high cell density by activating csgBA transcription.
CC Low-level constitutive expression confers an adherent curli fimbriae-
CC expressing phenotype, up-regulates 10 genes and down-regulates 14
CC others. {ECO:0000269|PubMed:16513732}.
CC -!- INTERACTION:
CC P52106; P52106: csgD; NbExp=3; IntAct=EBI-555538, EBI-555538;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:16513732}; Peripheral membrane protein
CC {ECO:0000305|PubMed:16513732}. Note=In experiments done with low-level
CC constitutively expressed protein.
CC -!- INDUCTION: Regulation is very complex. Strongly induced at 28 degrees
CC Celsius (at protein level), transcription regulation requires c-di-GMP,
CC although the mechanism is currently unknown. c-di-GMP levels are
CC stimulated by the diguanylate cyclase DgcM and repressed by the c-di-
CC GMP phosphodiesterase PdeR (YciR) (PubMed:17010156). Transcription
CC directly repressed by MqsA, and indirectly repressed by MqsA via MqsA's
CC repression of rpoS (PubMed:24212724). {ECO:0000269|PubMed:17010156,
CC ECO:0000269|PubMed:24212724}.
CC -!- DISRUPTION PHENOTYPE: No curli production.
CC {ECO:0000269|PubMed:24212724}.
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DR EMBL; X90754; CAA62280.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74124.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35830.1; -; Genomic_DNA.
DR EMBL; AF081826; AAD16025.1; -; Genomic_DNA.
DR PIR; S70786; S70786.
DR RefSeq; NP_415558.1; NC_000913.3.
DR RefSeq; WP_000481509.1; NZ_SSZK01000058.1.
DR AlphaFoldDB; P52106; -.
DR SMR; P52106; -.
DR BioGRID; 4260064; 9.
DR BioGRID; 853359; 1.
DR DIP; DIP-9328N; -.
DR IntAct; P52106; 2.
DR STRING; 511145.b1040; -.
DR jPOST; P52106; -.
DR PaxDb; P52106; -.
DR PRIDE; P52106; -.
DR EnsemblBacteria; AAC74124; AAC74124; b1040.
DR EnsemblBacteria; BAA35830; BAA35830; BAA35830.
DR GeneID; 949119; -.
DR KEGG; ecj:JW1023; -.
DR KEGG; eco:b1040; -.
DR PATRIC; fig|1411691.4.peg.1231; -.
DR EchoBASE; EB3186; -.
DR eggNOG; COG2197; Bacteria.
DR HOGENOM; CLU_000445_90_7_6; -.
DR OMA; AQTHLHE; -.
DR PhylomeDB; P52106; -.
DR BioCyc; EcoCyc:PD01379; -.
DR PRO; PR:P52106; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR CollecTF; EXPREG_00000b00; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CollecTF.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:EcoCyc.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IMP:CollecTF.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IPI:CollecTF.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:CollecTF.
DR GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; IMP:EcoCyc.
DR GO; GO:1900190; P:regulation of single-species biofilm formation; IDA:EcoCyc.
DR CDD; cd06170; LuxR_C_like; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF00196; GerE; 1.
DR PRINTS; PR00038; HTHLUXR.
DR SMART; SM00421; HTH_LUXR; 1.
DR SUPFAM; SSF46894; SSF46894; 1.
DR PROSITE; PS00622; HTH_LUXR_1; 1.
DR PROSITE; PS50043; HTH_LUXR_2; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; DNA-binding; Membrane;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..216
FT /note="CsgBAC operon transcriptional regulatory protein"
FT /id="PRO_0000184143"
FT DOMAIN 149..214
FT /note="HTH luxR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT DNA_BIND 173..192
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
SQ SEQUENCE 216 AA; 24935 MW; E1A5FD0DA1855DDE CRC64;
MFNEVHSIHG HTLLLITKSS LQATALLQHL KQSLAITGKL HNIQRSLDDI SSGSIILLDM
MEADKKLIHY WQDTLSRKNN NIKILLLNTP EDYPYRDIEN WPHINGVFYS MEDQERVVNG
LQGVLRGECY FTQKLASYLI THSGNYRYNS TESALLTHRE KEILNKLRIG ASNNEIARSL
FISENTVKTH LYNLFKKIAV KNRTQAVSWA NDNLRR
