DGCN_ECOLI
ID DGCN_ECOLI Reviewed; 408 AA.
AC P46139; P76598; P77005;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Diguanylate cyclase DgcN {ECO:0000305};
DE Short=DGC {ECO:0000305};
DE EC=2.7.7.65 {ECO:0000269|PubMed:27507823};
GN Name=dgcN {ECO:0000303|PubMed:26148715}; Synonyms=yfiN;
GN OrderedLocusNames=b2604, JW2585;
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 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
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], AND SEQUENCE REVISION.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 330-408.
RX PubMed=6357787; DOI=10.1002/j.1460-2075.1983.tb01519.x;
RA Bystroem A.S., Hjalmarsson K.J., Wikstroem P.M., Bjoerk G.R.;
RT "The nucleotide sequence of an Escherichia coli operon containing genes for
RT the tRNA(m1G)methyltransferase, the ribosomal proteins S16 and L19 and a
RT 21-K polypeptide.";
RL EMBO J. 2:899-905(1983).
RN [5]
RP IDENTIFICATION.
RX PubMed=7567469; DOI=10.1093/nar/23.17.3554;
RA Borodovsky M., McIninch J., Koonin E.V., Rudd K.E., Medigue C., Danchin A.;
RT "Detection of new genes in a bacterial genome using Markov models for three
RT gene classes.";
RL Nucleic Acids Res. 23:3554-3562(1995).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
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).
RN [7]
RP INDUCTION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=19332833; DOI=10.1099/mic.0.024257-0;
RA Sommerfeldt N., Possling A., Becker G., Pesavento C., Tschowri N.,
RA Hengge R.;
RT "Gene expression patterns and differential input into curli fimbriae
RT regulation of all GGDEF/EAL domain proteins in Escherichia coli.";
RL Microbiology 155:1318-1331(2009).
RN [8]
RP ROLE IN MOTILITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=20303158; DOI=10.1016/j.cell.2010.01.018;
RA Boehm A., Kaiser M., Li H., Spangler C., Kasper C.A., Ackermann M.,
RA Kaever V., Sourjik V., Roth V., Jenal U.;
RT "Second messenger-mediated adjustment of bacterial swimming velocity.";
RL Cell 141:107-116(2010).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=21181144; DOI=10.1007/s00253-010-3074-5;
RA Sanchez-Torres V., Hu H., Wood T.K.;
RT "GGDEF proteins YeaI, YedQ, and YfiN reduce early biofilm formation and
RT swimming motility in Escherichia coli.";
RL Appl. Microbiol. Biotechnol. 90:651-658(2011).
RN [10]
RP NOMENCLATURE.
RX PubMed=26148715; DOI=10.1128/jb.00424-15;
RA Hengge R., Galperin M.Y., Ghigo J.M., Gomelsky M., Green J., Hughes K.T.,
RA Jenal U., Landini P.;
RT "Systematic nomenclature for GGDEF and EAL domain-containing cyclic di-GMP
RT turnover proteins of Escherichia coli.";
RL J. Bacteriol. 198:7-11(2015).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, INTERACTION
RP WITH FTSZ AND ZIPA, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 329-ASP-GLU-330.
RX PubMed=27507823; DOI=10.1128/mbio.00822-16;
RA Kim H.K., Harshey R.M.;
RT "A diguanylate cyclase acts as a cell division inhibitor in a two-step
RT response to reductive and envelope stresses.";
RL MBio 7:E00822-E00822(2016).
CC -!- FUNCTION: Bifunctional protein that catalyzes the synthesis of cyclic-
CC di-GMP (c-di-GMP) in response to reductive stress and then dynamically
CC relocates to the division site to arrest cell division in response to
CC envelope stress. In the presence of high intracellular c-di-GMP levels,
CC and in response to envelope stress, interacts with cell division
CC proteins and halts cell division, without disassembling the Z ring, but
CC by blocking its further progress toward cytokinesis (PubMed:27507823).
CC Part of a network that regulates cell motility by altering levels of c-
CC di-GMP (PubMed:20303158). {ECO:0000269|PubMed:20303158,
CC ECO:0000269|PubMed:27507823}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 GTP = cyclic di-3',5'-guanylate + 2 diphosphate;
CC Xref=Rhea:RHEA:24898, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:58805; EC=2.7.7.65;
CC Evidence={ECO:0000269|PubMed:27507823};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P31129};
CC Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000250|UniProtKB:P31129};
CC -!- ACTIVITY REGULATION: Inhibited by YfiR, which prevents relocation to
CC the midcell. A reductive stress signal is required to inactivate YfiR
CC and turn on the DGC activity of DgcN. {ECO:0000269|PubMed:27507823}.
CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic di-GMP biosynthesis.
CC {ECO:0000305}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts with the cell division
CC proteins FtsZ and ZipA (PubMed:27507823). {ECO:0000269|PubMed:27507823,
CC ECO:0000305|PubMed:27507823}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localizes to the midcell in a Z ring-dependent
CC manner in response to cell envelope stress.
CC {ECO:0000269|PubMed:27507823}.
CC -!- INDUCTION: Expressed at low levels at both 28 and 37 degrees Celsius
CC during transition into stationary phase. {ECO:0000269|PubMed:19332833}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene increases swimming motility
CC and early biofilm formation (PubMed:21181144). Disruption partially
CC suppresses the reduced motility of a pdeH disruption; concomitant
CC disruption of dosC, dgcE, dgcQ and dgcN completely restores motility,
CC suggesting these 4 genes, together with the c-di-GMP phosphodiesterase
CC PdeH, form a network that regulates cell motility by altering levels of
CC c-di-GMP (PubMed:20303158). {ECO:0000269|PubMed:20303158,
CC ECO:0000269|PubMed:21181144}.
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DR EMBL; U00096; AAC75653.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16489.2; -; Genomic_DNA.
DR EMBL; X01818; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; G65038; G65038.
DR RefSeq; NP_417095.1; NC_000913.3.
DR RefSeq; WP_000969032.1; NZ_LN832404.1.
DR AlphaFoldDB; P46139; -.
DR SMR; P46139; -.
DR BioGRID; 4263361; 13.
DR STRING; 511145.b2604; -.
DR PaxDb; P46139; -.
DR PRIDE; P46139; -.
DR EnsemblBacteria; AAC75653; AAC75653; b2604.
DR EnsemblBacteria; BAA16489; BAA16489; BAA16489.
DR GeneID; 66673507; -.
DR GeneID; 947091; -.
DR KEGG; ecj:JW2585; -.
DR KEGG; eco:b2604; -.
DR PATRIC; fig|1411691.4.peg.4135; -.
DR EchoBASE; EB2718; -.
DR eggNOG; COG2199; Bacteria.
DR HOGENOM; CLU_039310_2_0_6; -.
DR InParanoid; P46139; -.
DR OMA; RVYADHN; -.
DR PhylomeDB; P46139; -.
DR BioCyc; EcoCyc:EG12880-MON; -.
DR BioCyc; MetaCyc:EG12880-MON; -.
DR BRENDA; 2.7.7.65; 2026.
DR UniPathway; UPA00599; -.
DR PRO; PR:P46139; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032153; C:cell division site; IDA:EcoCyc.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0052621; F:diguanylate cyclase activity; IDA:EcoCyc.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043709; P:cell adhesion involved in single-species biofilm formation; IBA:GO_Central.
DR GO; GO:0036460; P:cellular response to cell envelope stress; IDA:EcoCyc.
DR GO; GO:1902201; P:negative regulation of bacterial-type flagellum-dependent cell motility; IMP:EcoCyc.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd01949; GGDEF; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR033417; CHASE8.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR Pfam; PF17152; CHASE8; 1.
DR Pfam; PF00990; GGDEF; 1.
DR SMART; SM00267; GGDEF; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR TIGRFAMs; TIGR00254; GGDEF; 1.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; GTP-binding; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Reference proteome; Stress response;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..408
FT /note="Diguanylate cyclase DgcN"
FT /id="PRO_0000169270"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..52
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..112
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..154
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..408
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT DOMAIN 183..236
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 278..408
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT ACT_SITE 329
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 286
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 329
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT SITE 291
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
FT MUTAGEN 329..330
FT /note="DE->AA: Fails to localize to the midcell when
FT exposed to osmotic upshift."
FT /evidence="ECO:0000269|PubMed:27507823"
SQ SEQUENCE 408 AA; 45989 MW; 720B6539EF43DB16 CRC64;
MMDNDNSLNK RPTFKRALRN ISMTSIFITM MLIWLLLSVT SVLTLKQYAQ KNLALTAATM
TYSLEAAVVF ADGPAATETL AALGQQGQFS TAEVRDKQQN ILASWHYTRK DPGDTFSNFI
SHWLFPAPII QPIRHNGETI GEVRLTARDS SISHFIWFSL AVLTGCILLA SGIAITLTRH
LHNGLVEALK NITDVVHDVR SNRNFSRRVS EERIAEFHRF ALDFNSLLDE MEEWQLRLQA
KNAQLLRTAL HDPLTGLANR AAFRSGINTL MNNSDARKTS ALLFLDGDNF KYINDTWGHA
TGDRVLIEIA KRLAEFGGLR HKAYRLGGDE FAMVLYDVQS ESEVQQICSA LTQIFNLPFD
LHNGHQTTMT LSIGYAMTIE HASAEKLQEL ADHNMYQAKH QRAEKLVR
