ID A8AN42_CITK8 Unreviewed; 528 AA.
AC A8AN42;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=cyclic-guanylate-specific phosphodiesterase {ECO:0000256|ARBA:ARBA00012282};
DE EC=3.1.4.52 {ECO:0000256|ARBA:ARBA00012282};
GN OrderedLocusNames=CKO_03829 {ECO:0000313|EMBL:ABV14905.1};
OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=290338 {ECO:0000313|EMBL:ABV14905.1, ECO:0000313|Proteomes:UP000008148};
RN [1] {ECO:0000313|EMBL:ABV14905.1, ECO:0000313|Proteomes:UP000008148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696
RC {ECO:0000313|Proteomes:UP000008148};
RG The Citrobacter koseri Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (AUG-2007) 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}.
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DR EMBL; CP000822; ABV14905.1; -; Genomic_DNA.
DR RefSeq; WP_012134600.1; NC_009792.1.
DR AlphaFoldDB; A8AN42; -.
DR STRING; 290338.CKO_03829; -.
DR GeneID; 45137506; -.
DR KEGG; cko:CKO_03829; -.
DR HOGENOM; CLU_000445_131_1_6; -.
DR OrthoDB; 9812358at2; -.
DR Proteomes; UP000008148; Chromosome.
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:SF60; CYCLIC DI-GMP PHOSPHODIESTERASE PDEC-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, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008148};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 268..520
FT /note="EAL"
FT /evidence="ECO:0000259|PROSITE:PS50883"
SQ SEQUENCE 528 AA; 60507 MW; C43B874CC5B1A981 CRC64;
MNHSAQRKLL RFLGTIMVVL LPVMLALWFA HMRAVSETRN QLHSFAELAL EKTELVVQQV
ELARDAIQQY QGKACTPAHQ KRMQDIIRGR LYISELIYAQ DDHFLCSTVM APASPYIIPA
ADYKREPDVS IYYYRDTPFF AGYKMTYMQR GHYVAVINPL SYSEVMSDDP TLAWGVYDTV
TNSFFSVSEQ ANVEQLLPLL HRDESTFQQN NRFYTIAHSE KRPIAIIVST DNARFYQNLY
HQATLTLPLG IICSIIVLLM WSRTREEYHS PRRLLQRAID KRQLRLYYQP IIDIQNEKCV
GAEALLRWPG FEGQVMSPAE FIPLAEKEGM IAQITDYVVE EVFNDLGHFL ASQPHLYISI
NLSASDFHSS RLIALIAEKA RQHSVLAQQI KVEVTERGFI DVPKTTPVIQ AFRQAGFEVA
IDDFGTGYSN LHNLYSLNVD ILKIDKSFID TLTTNSTSHL IAEHIIEMAQ SLHLKAIAEG
VETADQVNWL FKRGVQYCQG WYFAKAMPPQ AFIQWLQQSP ALLMQRGQ
//
