ID   PDEB_BORBU              Reviewed;         379 AA.
AC   O50161;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Cyclic di-GMP phosphodiesterase PdeB {ECO:0000305};
DE            EC=3.1.4.- {ECO:0000269|PubMed:21670168};
GN   Name=PdeB {ECO:0000303|PubMed:21670168}; OrderedLocusNames=BB_0374;
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, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   DISRUPTION PHENOTYPE.
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 GMP. {ECO:0000269|PubMed:21670168}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cyclic di-3',5'-guanylate + 2 H2O = 2 GMP + 2 H(+);
CC         Xref=Rhea:RHEA:52928, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58115, ChEBI:CHEBI:58805;
CC         Evidence={ECO:0000269|PubMed:21670168};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:21670168};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.9 nM for c-di-GMP {ECO:0000269|PubMed:21670168};
CC   -!- DISRUPTION PHENOTYPE: Mutant cells exhibit a significantly increased
CC       flex rate. Deletion does not significantly affect virulence in needle-
CC       inoculated mice, but mutants display a reduced ability to survive in
CC       ticks and they are unable to complete the mouse-tick-mouse infection
CC       cycle. {ECO:0000269|PubMed:21670168}.
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DR   EMBL; AE000783; AAC66766.1; -; Genomic_DNA.
DR   PIR; E70146; E70146.
DR   RefSeq; NP_212508.1; NC_001318.1.
DR   RefSeq; WP_002556969.1; NC_001318.1.
DR   AlphaFoldDB; O50161; -.
DR   SMR; O50161; -.
DR   STRING; 224326.BB_0374; -.
DR   PRIDE; O50161; -.
DR   EnsemblBacteria; AAC66766; AAC66766; BB_0374.
DR   GeneID; 56567802; -.
DR   KEGG; bbu:BB_0374; -.
DR   PATRIC; fig|224326.49.peg.769; -.
DR   HOGENOM; CLU_000445_92_2_12; -.
DR   OMA; LYKNCKH; -.
DR   Proteomes; UP000001807; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd00077; HDc; 1.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR037522; HD_GYP_dom.
DR   SMART; SM00471; HDc; 1.
DR   PROSITE; PS51832; HD_GYP; 1.
PE   1: Evidence at protein level;
KW   c-di-GMP; Hydrolase; Reference proteome.
FT   CHAIN           1..379
FT                   /note="Cyclic di-GMP phosphodiesterase PdeB"
FT                   /id="PRO_0000174396"
FT   DOMAIN          114..310
FT                   /note="HD-GYP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01176"
SQ   SEQUENCE   379 AA;  43457 MW;  55F854130DF48723 CRC64;
     MQNSESIIKN IKNSSYLIDK EFLVWPENAF IGDKNIELIE KWNLKSYIKE RKNFFSDDSV
     KKEYEEIHKK FNEEAISSYH VIISNLEEIY ENCKRNKKIY YQDIMPTVKK VIEFYKKQKK
     IFIKYFRIPK LSANYHIIHS VNTAILTVAL GNEMGLNNYK TVELCSIALL HKIGFLFIPS
     KISEKKEALT EEELEIIKKY PIISYKIAST SNLSRSICLT LLTHKENLDG TGYPKGLTSE
     NISIESNIIG AASAYSAIIL DKAYKKSFNS GASIIELIKD ADKKFDKRVL KLIINAISSC
     PLDFIVELND NSIAKIVDID ESNPNLPYIN YIIKNGKVID KNEQSSVQSI PNTNTGIKKI
     LNQNEIELIK NKYSLIDII