ID B0SJF3_LEPBP Unreviewed; 694 AA.
AC B0SJF3;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Bifunctional diguanylate cyclase/phosphodiesterase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=LEPBI_I0307 {ECO:0000313|EMBL:ABZ96451.1};
OS Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ96451.1, ECO:0000313|Proteomes:UP000001847};
RN [1] {ECO:0000313|EMBL:ABZ96451.1, ECO:0000313|Proteomes:UP000001847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Patoc 1 / ATCC 23582 / Paris
RC {ECO:0000313|Proteomes:UP000001847};
RX PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL PLoS ONE 3:E1607-E1607(2008).
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DR EMBL; CP000786; ABZ96451.1; -; Genomic_DNA.
DR RefSeq; WP_012387339.1; NC_010602.1.
DR AlphaFoldDB; B0SJF3; -.
DR STRING; 456481.LEPBI_I0307; -.
DR KEGG; lbi:LEPBI_I0307; -.
DR HOGENOM; CLU_000445_70_20_12; -.
DR OrthoDB; 310793at2; -.
DR BioCyc; LBIF456481:LEPBI_RS01500-MONOMER; -.
DR Proteomes; UP000001847; Chromosome I.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd01948; EAL; 1.
DR CDD; cd01949; GGDEF; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.20.20.450; EAL domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR NCBIfam; TIGR00254; GGDEF; 1.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR33121; CYCLIC DI-GMP PHOSPHODIESTERASE PDEF; 1.
DR PANTHER; PTHR33121:SF71; CYCLIC DI-GMP PHOSPHODIESTERASE PDEF; 1.
DR Pfam; PF00563; EAL; 1.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13426; PAS_9; 1.
DR SMART; SM00052; EAL; 1.
DR SMART; SM00267; GGDEF; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF141868; EAL domain-like; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50883; EAL; 1.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001847}.
FT DOMAIN 12..82
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 134..210
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 294..427
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT DOMAIN 436..690
FT /note="EAL"
FT /evidence="ECO:0000259|PROSITE:PS50883"
SQ SEQUENCE 694 AA; 79037 MW; DC19B21593A891DC CRC64;
MRNEPLGKNI LSGLTVKSLL SEYPNSFQVL DWEGNFVSVT DRFARFLEFE PKEIVGKSIL
NFTQEDDKEN TQNTFEGLGE NPNIVNFENR LVTKSKEEVW IIWLLIPLTD SKIILGFDRD
VTIQKDISFE FLLQQQKYKS IFDNLPMGIA ITDEKGKIVE TNKTARTYFD IQDGELLNRT
LNIRKYTLIQ PNGTKIYPRK SSLMRALRHK EVIRNLEIGM IKENKITWFD ILATPIPIEN
FGLAVAFLDI TQRRHAEEKI AYMAFFDQLT NLPNRNSLID KLFPIFEEAR RHGNLVGILA
IDLDNFKIIN DSRGHDFGDK IIKLVAYRIR ESIRVYDLIS RQGGDEFTVV LPDLSNERDA
AVISESILDA MTHPFVIDGE RIFVNISIGI ALYPTDGKDS NTLLKNADSA LNLAKSQGKN
CYVFFTEELQ TVVAERLEIE NRMRIAIIEN QFTLMYQPKI DLYTRKPVGV EALIRWRHPE
RGLISPNVFI PISEETGMIL AIGEWVIKSA IKTMREWKDH GVKDISMAVN ISTKQFKHER
LISTIAENLK LYKVDPHDLE VELTESSVME NADAAVRTMQ EIRKLGAKIA IDDFGTGYSS
LGYLKKLPIS SLKIDRSFVS EITTDKDSKT IIHAVSNLAH NLGLSVVAEG AETEEQVRLL
AESGVDQIQG FYFAKPMTSE DCLHFLKTEL GISD
//