DGCQ_SALPA
ID DGCQ_SALPA Reviewed; 570 AA.
AC Q5PLI4;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=SPA0883;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV76864.1; -; Genomic_DNA.
DR RefSeq; WP_001119832.1; NC_006511.1.
DR AlphaFoldDB; Q5PLI4; -.
DR SMR; Q5PLI4; -.
DR PRIDE; Q5PLI4; -.
DR EnsemblBacteria; AAV76864; AAV76864; SPA0883.
DR KEGG; spt:SPA0883; -.
DR HOGENOM; CLU_000445_11_23_6; -.
DR OMA; EWQAWHD; -.
DR UniPathway; UPA00599; -.
DR UniPathway; UPA00694; -.
DR Proteomes; UP000008185; 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..570
FT /note="Probable diguanylate cyclase DgcQ"
FT /id="PRO_0000248035"
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; 65480 MW; B5A631E03C12A787 CRC64;
MPHETLLDNQ GWFKKLARRF GPGHVVNTCF LIVMLFSTLL TWREVMILKD AYVASQRNHL
GSVANVLDRQ LQFNMDRLIF LRNGMHEALV APLAFSALQS AVTQFEQRRV RHFWQLELDK
RRTLPLYGVS DQFVARTTLL SRESRDLANE LTATLELGYL ARLARSSAML TLETMYVSRS
GFYLSTLPTA YGSDIVSRYY QYVTQPWFIE QSQRRNPQRG VRWFTSAQPY VTDEQKKVTA
SLPLDHDNYW YGVLAMDIPV ASLQRFLRDA AEKDIEGEYQ LYDNHLRLLT DSAPEQQTAN
TLNDRERALL AREIEKDTLG GLRLGTHYVS WERLDHFDGV LLRVHTLREG IQGNFGSISI
ALTLLWVLFT AMLLISWGVI RHIVKNMFVL QNSLQWQAWH DPLTRLYNRG ALFEKASRLA
KRYREARQPF SVIQLDLDYF KSVNDRFGHQ AGDRVLSHAA GLIGSTIRAH DIAGRVGGEE
FCIVLPGATK AQALQIAERI RQRINDKEIL VTKSTTLRIS ASMGISSAEE YGDYDFEQLQ
SLADKRLYYA KQSGRNRICA SDATQEREKK
