DGCQ_SALTY
ID DGCQ_SALTY Reviewed; 570 AA.
AC Q8ZNT5;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=STM1987;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; AE006468; AAL20897.1; -; Genomic_DNA.
DR RefSeq; NP_460938.1; NC_003197.2.
DR RefSeq; WP_001119821.1; NC_003197.2.
DR AlphaFoldDB; Q8ZNT5; -.
DR SMR; Q8ZNT5; -.
DR STRING; 99287.STM1987; -.
DR PaxDb; Q8ZNT5; -.
DR EnsemblBacteria; AAL20897; AAL20897; STM1987.
DR GeneID; 1253508; -.
DR KEGG; stm:STM1987; -.
DR PATRIC; fig|99287.12.peg.2103; -.
DR HOGENOM; CLU_000445_11_23_6; -.
DR OMA; EWQAWHD; -.
DR PhylomeDB; Q8ZNT5; -.
DR BioCyc; SENT99287:STM1987-MON; -.
DR BRENDA; 2.7.7.65; 5542.
DR UniPathway; UPA00599; -.
DR UniPathway; UPA00694; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0052621; F:diguanylate cyclase activity; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043709; P:cell adhesion involved in single-species biofilm formation; IBA:GO_Central.
DR GO; GO:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1902201; P:negative regulation of bacterial-type flagellum-dependent cell motility; IBA:GO_Central.
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; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..570
FT /note="Probable diguanylate cyclase DgcQ"
FT /id="PRO_0000169100"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 428..563
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT ACT_SITE 479
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 436
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 444
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 449
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 453
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 479
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT SITE 441
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
SQ SEQUENCE 570 AA; 65430 MW; BF8FDF0CF8949925 CRC64;
MPHETLLDNQ GWFKKLARRF GPGHVVNTCF LIVMLFSTLL TWREVMILKD AYVASQRNHL
GSVANVLDRQ LQFNMDRLIF LRNGMHEALV APLAFSALQS AVTQFEQRRV RHFWQLELDK
RRTLPLYGVS DQFVARTTLL SRESRDLANE LTATLELGYL ARLARSSAML ALETMYVSRS
GFYLSTLPTA YGSDIVSRYY QYVTQPWFIE QSQRRNSQRG VRWFTSAQPY VTDEQKKVTA
SLPLDHDNYW YGVLAMDIPV ASLQRFLRDA AEKDIEGEYQ LYDNHLRLLT DSAPEQQTAN
TLNDRERALL AREIEKDTLG GLRLGTHYVS WERLDHFDGI LLRVHTLREG IQGNFGSISI
ALTLLWGLFT AMLLISWGVI RHMVKNMFVL QNSLQWQAWH DPLTRLYNRG ALFEKASRLA
KRYREARQPF SVIQLDLDYF KSVNDRFGHQ AGDRVLSHAA GLIGSTIRAH DIAGRVGGEE
FCIVLPGATK AQALQIAERI RQRINDKEIL VTKSTTLRIS ASMGISSAEE YGDYDFEQLQ
SLADKRLYYA KQSGRNRICA SDATQEREKK
