ID   PDEA_BORBU              Reviewed;         670 AA.
AC   O51338;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Cyclic di-GMP phosphodiesterase PdeA {ECO:0000305};
DE            EC=3.1.4.52 {ECO:0000269|PubMed:20444101};
GN   Name=pdeA {ECO:0000303|PubMed:21670168};
GN   OrderedLocusNames=BB_0363 {ECO:0000312|EMBL:AAC66750.1};
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=20444101; DOI=10.1111/j.1365-2958.2010.07191.x;
RA   Sultan S.Z., Pitzer J.E., Miller M.R., Motaleb M.A.;
RT   "Analysis of a Borrelia burgdorferi phosphodiesterase demonstrates a role
RT   for cyclic-di-guanosine monophosphate in motility and virulence.";
RL   Mol. Microbiol. 77:128-142(2010).
RN   [3]
RP   GENE NAME.
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=21670168; DOI=10.1128/iai.05153-11;
RA   Sultan S.Z., Pitzer J.E., Boquoi T., Hobbs G., Miller M.R., Motaleb M.A.;
RT   "Analysis of the HD-GYP domain cyclic dimeric GMP phosphodiesterase reveals
RT   a role in motility and the enzootic life cycle of Borrelia burgdorferi.";
RL   Infect. Immun. 79:3273-3283(2011).
CC   -!- FUNCTION: Phosphodiesterase (PDE) that catalyzes the hydrolysis of
CC       cyclic diguanylate (c-di-GMP) to pGpG. {ECO:0000269|PubMed:20444101}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cyclic di-3',5'-guanylate + H2O = 5'-
CC         phosphoguanylyl(3'->5')guanosine + H(+); Xref=Rhea:RHEA:24902,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58754,
CC         ChEBI:CHEBI:58805; EC=3.1.4.52;
CC         Evidence={ECO:0000269|PubMed:20444101};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.054 uM for c-di-GMP {ECO:0000269|PubMed:20444101};
CC   -!- DISRUPTION PHENOTYPE: Inactivation results in altered motility. Mutants
CC       are able to survive in tick guts, but they are unable to establish an
CC       infection in mice. {ECO:0000269|PubMed:20444101}.
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DR   EMBL; AE000783; AAC66750.1; -; Genomic_DNA.
DR   PIR; B70145; B70145.
DR   RefSeq; NP_212497.1; NC_001318.1.
DR   RefSeq; WP_002665233.1; NC_001318.1.
DR   AlphaFoldDB; O51338; -.
DR   SMR; O51338; -.
DR   STRING; 224326.BB_0363; -.
DR   EnsemblBacteria; AAC66750; AAC66750; BB_0363.
DR   KEGG; bbu:BB_0363; -.
DR   PATRIC; fig|224326.49.peg.758; -.
DR   HOGENOM; CLU_413710_0_0_12; -.
DR   OMA; MSFYSEY; -.
DR   Proteomes; UP000001807; Chromosome.
DR   GO; GO:0071111; F:cyclic-guanylate-specific phosphodiesterase activity; IEA:UniProtKB-EC.
DR   CDD; cd01948; EAL; 1.
DR   Gene3D; 3.20.20.450; -; 1.
DR   InterPro; IPR001633; EAL_dom.
DR   InterPro; IPR035919; EAL_sf.
DR   Pfam; PF00563; EAL; 1.
DR   SMART; SM00052; EAL; 1.
DR   SUPFAM; SSF141868; SSF141868; 1.
DR   PROSITE; PS50883; EAL; 1.
PE   1: Evidence at protein level;
KW   c-di-GMP; Hydrolase; Reference proteome.
FT   CHAIN           1..670
FT                   /note="Cyclic di-GMP phosphodiesterase PdeA"
FT                   /id="PRO_0000440639"
FT   DOMAIN          428..670
FT                   /note="EAL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00074"
SQ   SEQUENCE   670 AA;  78210 MW;  F8A60F8FFE219942 CRC64;
     MNKVNNYQNI NSVIISKKEV GLRDLIKLKS IFNLIQIVKS EKALYSEYVK QNNIKFAIIY
     NYEKPIDFSI NIANELKNAN KIHSIIISKE KFDEEYLKLD HIEIIKDISE LEYKQSLIHQ
     KKLFCDNKNT TLDFFLNLSE LIKEIVIITN TKNEIIYINE KGSKNLNLPM KTSGNIIKVT
     DIDIRDWEKL EKINLSYHTN SIPEFKNILI TDCLLTLKNN KKLHVDIFIS TIAQNNIDKL
     ITIKEISNSN KIENYKYLEI IDSQDEIQNA KEIEKLLVNH MDIYKKKSIY LLNLDVSLTA
     EYEYKEDQEK LNAKILKIMY SKIMSLYSEY IFKLKHNNLI VIISTSGGEK RIISIAKKIK
     KTIALAFKKE DIIIFKFNIG IIEVNLKENL EFKIPKLMMA TKISSEYKES NPTIYKEELP
     EAVILKNQNK IFQYILKAIK NDFFTLYYQK INPLKKNLKP KIEILTRLFD HMGKPIPNNQ
     IFNLIDKYNL TVEVDTLVVK KALREYKSFV SKNGIHIFSI NISPYSLKSQ NFRIFLRDTL
     LKSQIPLQNI CLEITETGIL ENFEIINKYF QELKSFGIKL ALDDFGSGHT SLSYIKTLPI
     DLLKIDGSFI KAINSSEIDF VIIKSIKKIA DTKNIKIIAE FVYNEEILKK IIELEIDYGQ
     GFLWHKPEPI