ID W1X2J1_ECOLX Unreviewed; 532 AA.
AC W1X2J1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=cyclic-guanylate-specific phosphodiesterase {ECO:0000256|ARBA:ARBA00012282};
DE EC=3.1.4.52 {ECO:0000256|ARBA:ARBA00012282};
GN ORFNames=Q609_ECAC01583G0007 {ECO:0000313|EMBL:ETJ22939.1};
OS Escherichia coli DORA_A_5_14_21.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=1403943 {ECO:0000313|EMBL:ETJ22939.1, ECO:0000313|Proteomes:UP000018853};
RN [1] {ECO:0000313|EMBL:ETJ22939.1, ECO:0000313|Proteomes:UP000018853}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DORA_A_5_14_21 {ECO:0000313|Proteomes:UP000018853};
RA Brown C.T., Sharon I., Thomas B.C., Castelle C.J., Morowitz M.J.,
RA Banfield J.F.;
RT "A Varibaculum cambriense genome reconstructed from a premature infant gut
RT community with otherwise low bacterial novelty that shifts toward anaerobic
RT metabolism during the third week of life.";
RL Submitted (DEC-2013) 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:ETJ22939.1}.
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DR EMBL; AZLZ01001583; ETJ22939.1; -; Genomic_DNA.
DR AlphaFoldDB; W1X2J1; -.
DR PATRIC; fig|1403943.3.peg.2899; -.
DR Proteomes; UP000018853; 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:SF9; CYCLIC DI-GMP PHOSPHODIESTERASE PDED-RELATED; 1.
DR PANTHER; PTHR33121; CYCLIC DI-GMP PHOSPHODIESTERASE PDEF; 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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 266..515
FT /note="EAL"
FT /evidence="ECO:0000259|PROSITE:PS50883"
SQ SEQUENCE 532 AA; 59667 MW; 9EA79F84BA909BCF CRC64;
MQKAQRIIKT YRRNRMIVCT ICALVTLAST LSVRFISQRN LNQQRVVQFA NHAVEELDKV
LLPLQAGSEV LLPLIGLPCS VAHLPLRKQA AKLQTVRSIG LVQDGTLYCS SIFGYRNVPV
VDILAELPAP QPLLRLTIDR ALIKGSPVLI QWTPAAGSSN AGVMEMINID LLAAMLLEPQ
LPQISSASLT VDNRHLLYGN GLVDTLPQPE DNENYQVSSQ RFPFTINVNG PGATALAWHY
LPTQLPLAVL LSLLVGYIAW LATAYRMSFS REINLGLAQH EFELFCQPLL NARSQQCIGV
EILLRWNNPR QGWISPDVFI PIAEEHHLIV PLTRYVMAET IRQRHVFPMS SQFHVGINVA
PSHFRRGVLI KDLNQYWFSA HPIQQLILEI TERDALLDVD YRIARELHRK NVKLAIDDFG
TGNSSFSWLE TLRPDVLKID KSFTAAIGSD AVNSTVTDII IALGQRLNIE LVAEGVETQE
QAKYLRRHGV HILQGYLYAQ PMPLRDFPKW LAGSQPPPAR HNGHITPVMP LR
//
