DGCQ_SALTI
ID DGCQ_SALTI Reviewed; 567 AA.
AC Q8Z5R0;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=STY2194, t0891;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD05734.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO68569.1; -; Genomic_DNA.
DR RefSeq; NP_456547.1; NC_003198.1.
DR RefSeq; WP_001119838.1; NZ_UCTX01000001.1.
DR AlphaFoldDB; Q8Z5R0; -.
DR SMR; Q8Z5R0; -.
DR STRING; 220341.16503227; -.
DR EnsemblBacteria; AAO68569; AAO68569; t0891.
DR KEGG; stt:t0891; -.
DR KEGG; sty:STY2194; -.
DR PATRIC; fig|220341.7.peg.2210; -.
DR eggNOG; COG3706; Bacteria.
DR HOGENOM; CLU_000445_11_23_6; -.
DR OMA; EWQAWHD; -.
DR UniPathway; UPA00599; -.
DR UniPathway; UPA00694; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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..567
FT /note="Probable diguanylate cyclase DgcQ"
FT /id="PRO_0000169099"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 425..560
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT ACT_SITE 476
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 433
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 441
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 446
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 450
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 476
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT SITE 438
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
SQ SEQUENCE 567 AA; 65099 MW; 9E1AE3768ADADF6D CRC64;
MPHETLLDNQ GWFKKLARRF GPGHVVNTCF LIVMLFSTLL TWREVMILKD AYVASQRNHL
GSVANVLDRQ LQFNMDRLIF LRNGMHEALV APLAFSALQS AVTQFEQRRV RHFWQLELDK
RRTLPLYGVS DQFVARTTLL SRESRDLANE LTATLELGYL ARSSAMLTLE TMYVSRSGFY
LSTLPTAYGS DIVSRYYQYV TQPWFIEQSQ RRNPQRGVRW FTSAQPYVAD EQKKVTASLP
LDHDNYWYGV LAMDIPVASL QQFLRDAAEK DIEGEYQLYD NHLRLLTDSA PEQQTENTLN
DRERALLARE IEKDTLGGLR LGTHYVSWER LDHFDGVLLR VHTLREGIQG NFGSISIALT
LLWGLFTAML LISWGVIRHM VKNMFVLQNS PQWQAWHDPL TRLYNRGALF EKASRLAKRY
REARQPFSVI QLDLDYFKSV NDRFGHQAGD RVLSHAAGLI GSTIRAHDIA GRVGGEEFCI
VLPGATKAQA LQIAERIRQR INDKEILVTK STTLRISASM GISSAEEYGD YDFEQLQSLA
DKRLYYAKQS GRNRICASDA TQEREKK
