DGCQ_SHIFL
ID DGCQ_SHIFL Reviewed; 569 AA.
AC Q83KM9;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Putative 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=SF2000, S2095;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(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}.
CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN43546.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE005674; AAN43546.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE014073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_707839.1; NC_004337.2.
DR AlphaFoldDB; Q83KM9; -.
DR SMR; Q83KM9; -.
DR STRING; 198214.SF2000; -.
DR EnsemblBacteria; AAN43546; AAN43546; SF2000.
DR GeneID; 1025207; -.
DR KEGG; sfl:SF2000; -.
DR PATRIC; fig|198214.7.peg.2389; -.
DR HOGENOM; CLU_000445_11_23_6; -.
DR UniPathway; UPA00599; -.
DR UniPathway; UPA00694; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 5: Uncertain;
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..569
FT /note="Putative diguanylate cyclase DgcQ"
FT /id="PRO_0000248037"
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; 64825 MW; D6880B5A022A7B06 CRC64;
MGVVRVQHET KMENQSWLKK LARRLGPGHV VNLCFIVVLL FSTLLTWREV VVLEDAYISS
QRNHLENVAN ALDKHLQYNV DKLIFLRNGM REALVAPLDF TSLRNAVTEF EQHRDEHAWQ
IELNRRRTLP VNGVSDALVS EGNFLSRENE SLDNEITAAL EVGYLLRLAH NSSSMVEQAM
YVSRAGFYVS TQPTLFTRNV PTRYYGYVTQ PWFIGHSQRE NRHRAVRWFT SQPEHASNTE
PQVTVSVPVD SNNYWYGVLG MSIPVRTMQQ FLRNAIDKNL DGEYQLYDSK LRFLTSSNPD
HPTGNIFDPR ELALLAQAME HDTRGGIRMD SRYVSWERLD HFDGVLARVH TLSEGVRGDF
GSISIALTLL WALFTTMLLL SWYVIRRMVS NMYVLQSSLQ WQAWHDTLTR LYNRGALFEK
ARPLAKLCQT HQHPFSVIQV DLDHFKAIND RFGHQAGDRV LSHAAGLISS SLRAQDVAGR
VGGEEFCVIL PGANLTQAAE VAERIRLKLN EKEMLIAKST TIRISASLGV SSSEETGDYD
FEQLQSLADR RLYLAKQAGR NRVFASDNA
