DOSC_SHIFL
ID DOSC_SHIFL Reviewed; 381 AA.
AC Q83KV7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
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; Synonyms=yddV; OrderedLocusNames=SF1736.1, S1869.1;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN43312.1; -; Genomic_DNA.
DR EMBL; AE014073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_707605.1; NC_004337.2.
DR RefSeq; WP_005062918.1; NZ_WPGW01000136.1.
DR AlphaFoldDB; Q83KV7; -.
DR SMR; Q83KV7; -.
DR STRING; 198214.SF1737; -.
DR EnsemblBacteria; AAN43312; AAN43312; SF1737.
DR GeneID; 1024899; -.
DR GeneID; 58391398; -.
DR KEGG; sfl:SF1737; -.
DR PATRIC; fig|198214.7.peg.2058; -.
DR HOGENOM; CLU_000445_11_5_6; -.
DR OMA; DGHPDYE; -.
DR OrthoDB; 1635706at2; -.
DR UniPathway; UPA00599; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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..381
FT /note="Diguanylate cyclase DosC"
FT /id="PRO_0000316155"
FT DOMAIN 325..381
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
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 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 381 AA; 43997 MW; 1A279976A2F189C2 CRC64;
MEMYFKRMKD EWTGLVEQAD PLIRAKAAEI ALAHAHYLSI EFYRIVRIDP HAEEFLSNEQ
VERQLKSAME RWIINVLSAQ VDDVERLIQI QHTVAEVHAR IGIPVEIVEM GFRVLKKILY
PVIFSSDYSA AEKLQVYHFS INSIDIAMEV MTRAFTFSDS SASKEDENYR IFSLLENAEE
EKERQIASIL SWEIDIIYKV LLDSDLGSSL PLSQADFGLW FNHKGRHYFS GIAEVGHISR
LIQDFDGIFN QTMRNTRILN NRSLRVKFLL QIRNTVSQII TLLRELFEEV SRHEVGMDVL
TKLLNRRFLP TIFKREIAHA NRTGTPLSVL IIDVDKFKEI NDTWGHNTGD EILRKVSFLS
QKRLVKSKIL GAGSSRKLAV S
