ID A0A0J6NEJ2_9NEIS Unreviewed; 535 AA.
AC A0A0J6NEJ2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=cyclic-guanylate-specific phosphodiesterase {ECO:0000256|ARBA:ARBA00012282};
DE EC=3.1.4.52 {ECO:0000256|ARBA:ARBA00012282};
GN ORFNames=VK98_22405 {ECO:0000313|EMBL:KMN76159.1};
OS Chromobacterium sp. LK11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Chromobacterium.
OX NCBI_TaxID=1628212 {ECO:0000313|EMBL:KMN76159.1, ECO:0000313|Proteomes:UP000036114};
RN [1] {ECO:0000313|EMBL:KMN76159.1, ECO:0000313|Proteomes:UP000036114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LK11 {ECO:0000313|EMBL:KMN76159.1,
RC ECO:0000313|Proteomes:UP000036114};
RA Chan X.Y.;
RT "Draft genome of Chromobacterium aquaticum LK11.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',3'-c-di-GMP + H2O = 5'-phosphoguanylyl(3'->5')guanosine +
CC H(+); Xref=Rhea:RHEA:24902, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58754, ChEBI:CHEBI:58805; EC=3.1.4.52;
CC Evidence={ECO:0000256|ARBA:ARBA00034290};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMN76159.1}.
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DR EMBL; LDUR01000053; KMN76159.1; -; Genomic_DNA.
DR RefSeq; WP_048416132.1; NZ_LDUR01000053.1.
DR AlphaFoldDB; A0A0J6NEJ2; -.
DR STRING; 1628212.VK98_22405; -.
DR PATRIC; fig|1628212.3.peg.4073; -.
DR Proteomes; UP000036114; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0071111; F:cyclic-guanylate-specific phosphodiesterase activity; IEA:UniProtKB-EC.
DR CDD; cd01948; EAL; 1.
DR Gene3D; 3.20.20.450; EAL domain; 1.
DR InterPro; IPR024744; CSS-motif_dom.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR PANTHER; PTHR33121; CYCLIC DI-GMP PHOSPHODIESTERASE PDEF; 1.
DR PANTHER; PTHR33121:SF80; CYCLIC DI-GMP PHOSPHODIESTERASE PDEL-RELATED; 1.
DR Pfam; PF12792; CSS-motif; 1.
DR Pfam; PF00563; EAL; 1.
DR SMART; SM00052; EAL; 1.
DR SUPFAM; SSF141868; EAL domain-like; 1.
DR PROSITE; PS50883; EAL; 1.
PE 4: Predicted;
KW c-di-GMP {ECO:0000256|ARBA:ARBA00022636};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000036114};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 26..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 248..270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 273..525
FT /note="EAL"
FT /evidence="ECO:0000259|PROSITE:PS50883"
SQ SEQUENCE 535 AA; 59271 MW; 33C29A8927DF7053 CRC64;
MFCRHRFRHL ISRGNQFRGS LNAAEWTLVL LVAVLPAAVG LPLTWNRYQL DVQAQLQSAA
GRAVNSVDRV FGQVDRSLRE AAPLAGLPCP QARGQLVSLA AFDPYIRSLG LMDGRRLYCT
SVLGAQDTVL PFTPSAPQQL IHRQGSGPLY PKRPFLMRTL LTERGQGLVA SVELAYFSPL
LPWQADDGHS GSLLVLNHKE AVQSTLPGAA EVPASAVLRV IAASQRYPLA VHSWVDAKYL
WRGASARLLR ALLLLLPVGV VGAVLLLGYL RKRGSVSGEI LLALRNQEFL PYYQPVFDAC
GRRCMGVEVL LRWQHPRQGL APPDLFIPVA EASGMIIQIT RYLMRKVAAD MASLPLPERF
FVALNLSPSH LQHAQLVEDC QAFLQHFPKA PPRLVLEVTE REPIQVTPQS QQVMAALRRM
RVQIAIDDFG TGHSSLAELN RIHADHLKID RVFVAAIGSD SIANRILEMI IDLAKQLRIS
MVAEGVETEQ QRAYLQQSGV HYLQGYLLAR PMPLEQLRDF LWGRRAPLAE GQAAS
//
