DOSC_SHIF8
ID DOSC_SHIF8 Reviewed; 381 AA.
AC Q0T466;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=SFV_1733;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(2006).
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; CP000266; ABF03899.1; -; Genomic_DNA.
DR RefSeq; WP_005105493.1; NC_008258.1.
DR AlphaFoldDB; Q0T466; -.
DR SMR; Q0T466; -.
DR EnsemblBacteria; ABF03899; ABF03899; SFV_1733.
DR KEGG; sfv:SFV_1733; -.
DR HOGENOM; CLU_000445_11_5_6; -.
DR OMA; DGHPDYE; -.
DR BioCyc; SFLE373384:SFV_RS09670-MON; -.
DR UniPathway; UPA00599; -.
DR Proteomes; UP000000659; 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 Transferase.
FT CHAIN 1..381
FT /note="Diguanylate cyclase DosC"
FT /id="PRO_0000316156"
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; 43983 MW; 43BABDAEC04CC83A CRC64;
MEMYFKRMKD EWTGLVEQAD PLIRAKAAEI ALAHAHYLSI EFYRIVRIDP HAEEFLSNEQ
VERQLKSAME RWIINVLSAQ VDDVERLIQI QHTVAEVHAR IGIPVEIVEM GFRVLKKILY
PVIFSSDYSA AEKLQVYHFS INSIDIAMEV MTRAFTFSDS SASKEDENYR IFSLLENGEE
EKERQIASIL SWEIDIIYKV LLDSDLGSSL PLSQADFGLW FNHKGRHYFS GIAEVGHISR
LIQDFDGIFN QTMRNTRILN NRSLRVKFLL QIRNTVSQII TLLRELFEEV SRHEVGMDVL
TKLLNRRFLP TIFKREIAHA NRTGTPLSVL IIDVDKFKEI NDTWGHNTGD EILRKVSFLS
QKRLVKSKIL GAGSSRKLAV S
