DGCQ_SHISS
ID DGCQ_SHISS Reviewed; 569 AA.
AC Q3Z0N3;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Probable diguanylate cyclase DgcQ {ECO:0000250|UniProtKB:P76330};
DE Short=DGC {ECO:0000250|UniProtKB:P76330};
DE EC=2.7.7.65 {ECO:0000250|UniProtKB:P76330};
DE AltName: Full=Cellulose synthesis regulatory protein {ECO:0000250|UniProtKB:P76330};
GN Name=dgcQ {ECO:0000250|UniProtKB:P76330}; Synonyms=yedQ;
GN OrderedLocusNames=SSON_2013;
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
CC -!- FUNCTION: Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the
CC condensation of 2 GTP molecules (By similarity). Cyclic-di-GMP is a
CC second messenger which controls cell surface-associated traits in
CC bacteria. Involved in the regulation of cellulose production (By
CC similarity). {ECO:0000250|UniProtKB:P31129,
CC ECO:0000250|UniProtKB:P76330}.
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:P31129};
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: Glycan metabolism; bacterial cellulose biosynthesis.
CC {ECO:0000250|UniProtKB:P76330}.
CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic di-GMP biosynthesis.
CC {ECO:0000250|UniProtKB:P76330}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P31129}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
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DR EMBL; CP000038; AAZ88679.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3Z0N3; -.
DR SMR; Q3Z0N3; -.
DR EnsemblBacteria; AAZ88679; AAZ88679; SSON_2013.
DR KEGG; ssn:SSON_2013; -.
DR HOGENOM; CLU_000445_11_23_6; -.
DR OMA; EWQAWHD; -.
DR UniPathway; UPA00599; -.
DR UniPathway; UPA00694; -.
DR Proteomes; UP000002529; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 GO; GO:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd01949; GGDEF; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR033416; CHASE7.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR Pfam; PF17151; CHASE7; 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.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Cellulose biosynthesis; GTP-binding;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..569
FT /note="Probable diguanylate cyclase DgcQ"
FT /id="PRO_0000248038"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 433..568
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT ACT_SITE 484
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 441
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 449
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 454
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 458
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 484
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT SITE 446
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
SQ SEQUENCE 569 AA; 64752 MW; 6EB203368F1D432A CRC64;
MGVVRVQHET KMENQSWLKK LARRLGPGHV VNLCFIVVLL FSTLLTWREV VVLEDAYISS
QRNHLENVAN ALDKHLQYNV DKLIFLRNGM REALVAPLDF TSLRNAVTEF EQHRDEHAWQ
IELNRRRTLS VNGVSDALVS EGNLLSRENE SLDNEITAAL EVGYLLRLAH NTSSMVEQAM
YVSRAGFYVS TQPTLFTRNV PTRYYGYVTQ PWFIGHSQRE NRHRAVRWFT SQPEHASNTE
PQVTVSVPVD SNNYWYGVLG MSIPVRTMQQ FLRNAIDKNL DGEYQLYDSK LRFLTSSNPD
HPTGNIFDPR ELALLAQAME HDTRGGIRMD SRYVSWERLD HFDGVLVRVH TLSEGVRGDF
GSISIALTLL WALFTTMLLI SWYVIRRMVS NMYVLQSSLQ WQAWHDTLTR LYNRGALFEK
ARPLAKLCQT HQHPFSVIQV DLDHFKAIND RFGHQAGDRV LSHAAGLISS SLRAQDVAGR
VGGEEFCVIL PGASLTEAAE VAERIRLKLN EKEMLIAKST TIRISASLGV SSSEETGDYD
FEQLQSLADR RLYLAKQAGR NRVCASDNA
