DOSC_ECO57
ID DOSC_ECO57 Reviewed; 460 AA.
AC P0AA90; P77793;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Diguanylate cyclase DosC;
DE Short=DGC;
DE EC=2.7.7.65;
DE AltName: Full=Direct oxygen-sensing cyclase;
GN Name=dosC; OrderedLocusNames=Z2219, ECs2095;
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: Globin-coupled heme-based oxygen sensor protein displaying
CC diguanylate cyclase (DGC) activity in response to oxygen availability.
CC Thus, catalyzes the synthesis of cyclic diguanylate (c-di-GMP) via the
CC condensation of 2 GTP molecules. Cyclic-di-GMP is a second messenger
CC which controls cell surface-associated traits in bacteria (By
CC similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC Note=Binds 1 heme group per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic di-GMP biosynthesis.
CC -!- DOMAIN: Is composed of an N-terminal sensory globin-fold domain that
CC binds heme and oxygen, and a C-terminal GGDEF diguanylate cyclase
CC domain. {ECO:0000250}.
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DR EMBL; AE005174; AAG56278.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB35518.1; -; Genomic_DNA.
DR PIR; B85727; B85727.
DR PIR; G90890; G90890.
DR RefSeq; NP_310122.1; NC_002695.1.
DR RefSeq; WP_000426292.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AA90; -.
DR SMR; P0AA90; -.
DR STRING; 155864.EDL933_2150; -.
DR EnsemblBacteria; AAG56278; AAG56278; Z2219.
DR EnsemblBacteria; BAB35518; BAB35518; ECs_2095.
DR GeneID; 917293; -.
DR KEGG; ece:Z2219; -.
DR KEGG; ecs:ECs_2095; -.
DR PATRIC; fig|386585.9.peg.2200; -.
DR eggNOG; COG3706; Bacteria.
DR HOGENOM; CLU_000445_11_5_6; -.
DR OMA; DGHPDYE; -.
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:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR CDD; cd01949; GGDEF; 1.
DR CDD; cd14757; GS_EcDosC-like_GGDEF; 1.
DR Gene3D; 1.10.490.10; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR039435; DosC_GS.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR044398; Globin-sensor_dom.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF11563; Protoglobin; 1.
DR SMART; SM00267; GGDEF; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR TIGRFAMs; TIGR00254; GGDEF; 1.
DR PROSITE; PS50887; GGDEF; 1.
PE 3: Inferred from homology;
KW GTP-binding; Heme; Iron; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..460
FT /note="Diguanylate cyclase DosC"
FT /id="PRO_0000201322"
FT DOMAIN 325..458
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT ACT_SITE 376
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 98
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 376
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 43
FT /note="Involved in oxygen binding and important for the
FT stability of the Fe(II)-O(2) complex"
FT /evidence="ECO:0000250"
FT SITE 60
FT /note="Important for oxygen binding and stability of the
FT Fe(II)-O(2) complex"
FT /evidence="ECO:0000250"
FT SITE 65
FT /note="Critical for restricting water access to the heme
FT distal side to avoid rapid autoxidation"
FT /evidence="ECO:0000250"
FT SITE 338
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
SQ SEQUENCE 460 AA; 53178 MW; 79168311553E61C3 CRC64;
MEMYFKRMKD EWTGLVEQAD PPIRAKAAEI AVAHAHYLSI EFYRIVRIDP HAEEFLSNEQ
VERQLKSAME RWIINVLSAQ VDDVERLIQI QHTVAEVHAR IGIPVEIVEM GFRVLKKILY
PVIFSSDYSA AEKLQVYHFS INSIDIAMEV MTRAFTFSDS SASKEDENYR IFSLLENAEE
EKERQIASIL SWEIDIIYKI LLDSDLGSSL PLSQADFGLW FNHKGRHYFS GIAEVGHISR
LIQDFDGIFN QTMRNTRNLN NRSLRVKFLL QIRNTVSQII TLLRELFEEV SRHEVGMDVL
TKLLNRRFLP TIFKREIAHA NRTGTPLSVL IIDVDKFKEI NDTWGHNTGD EILRKVSQAF
YDNVRSSDYV FRYGGDEFII VLTEASENET LRTAERIRSR VEKTKLKAAN GEDIALSLSI
GAAMFNGHPD YERLIQIADE ALYIAKRRGR NRVELWKASL
