DGCM_ECO57
ID DGCM_ECO57 Reviewed; 410 AA.
AC Q8X8Q3;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Diguanylate cyclase DgcM {ECO:0000250|UniProtKB:P77302};
DE Short=DGC {ECO:0000250|UniProtKB:P77302};
DE EC=2.7.7.65 {ECO:0000250|UniProtKB:P77302};
GN Name=dgcM {ECO:0000250|UniProtKB:P77302}; Synonyms=ydaM;
GN OrderedLocusNames=Z2421, ECs1925;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Part of a signaling cascade that regulates curli
CC biosynthesis. The cascade is composed of two cyclic-di-GMP (c-di-GMP)
CC control modules, in which c-di-GMP controlled by the DgcE/PdeH pair
CC (module I) regulates the activity of the DgcM/PdeR pair (module II),
CC which in turn regulates activity of the transcription factor MlrA and
CC expression of the master biofilm regulator csgD.
CC {ECO:0000250|UniProtKB:P77302}.
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:0000250|UniProtKB:P77302};
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 -!- PATHWAY: Purine metabolism; 3',5'-cyclic di-GMP biosynthesis.
CC {ECO:0000250|UniProtKB:P77302}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG56456.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB35348.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005174; AAG56456.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB35348.1; ALT_INIT; Genomic_DNA.
DR PIR; D85749; D85749.
DR PIR; E90869; E90869.
DR RefSeq; NP_309952.2; NC_002695.1.
DR RefSeq; WP_000628061.1; NZ_SEKU01000010.1.
DR AlphaFoldDB; Q8X8Q3; -.
DR SMR; Q8X8Q3; -.
DR STRING; 155864.EDL933_2332; -.
DR EnsemblBacteria; AAG56456; AAG56456; Z2421.
DR EnsemblBacteria; BAB35348; BAB35348; ECs_1925.
DR GeneID; 912323; -.
DR KEGG; ece:Z2421; -.
DR KEGG; ecs:ECs_1925; -.
DR PATRIC; fig|386585.9.peg.2032; -.
DR eggNOG; COG3706; Bacteria.
DR HOGENOM; CLU_000445_11_4_6; -.
DR OMA; HTWEINT; -.
DR UniPathway; UPA00599; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0052621; F:diguanylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01949; GGDEF; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF08448; PAS_4; 1.
DR SMART; SM00267; GGDEF; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55073; SSF55073; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR TIGRFAMs; TIGR00254; GGDEF; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS50113; PAC; 1.
PE 3: Inferred from homology;
KW GTP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Repeat; Transferase.
FT CHAIN 1..410
FT /note="Diguanylate cyclase DgcM"
FT /id="PRO_0000201314"
FT DOMAIN 3..70
FT /note="PAS 1"
FT /evidence="ECO:0000255"
FT DOMAIN 129..198
FT /note="PAS 2"
FT /evidence="ECO:0000255"
FT DOMAIN 199..251
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 283..410
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT ACT_SITE 334
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 291
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 304
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 334
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT SITE 296
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
SQ SEQUENCE 410 AA; 46495 MW; 1B331C47E84DC8B5 CRC64;
MITHNFNTLD LLTSPVWIVS PFEEQLIYAN SAARLLMQDL TFSQLRTGPY SVSSQKELPK
YLSDLQNQHD IIEILTVQRK EEETALSCRL VLRELTETEP VIIFEGIEAP ATLGLKASRS
ANYQRKKQGF YARFFLTNSA PMLLIDPSRD GQIVDANLAA LNFYGYNHET MCQKHTWEIN
MLGRRVMPIM HEISHLPGGH KPLNFIHKLA DGSTRHVQTY AGPIEIYGDK LMLCIVHDIT
EQKRLEEQLE HAAHHDAMTG LLNRRQFYHI TEPGQMQHLA IAQDYSLLLI DTDRFKHIND
LYGHSKGDEV LCALARTLES CARKGDLVFR WGGEEFVLLL PRTPLDTALS LAETIRVSVA
KVSISGLPRF TVSIGVAHHE GNESIDELFK RVDDALYRAK NDGRNRVLAA
