(data stored in SCRATCH zone)

SWISSPROT: PGPH_BACSU

ID   PGPH_BACSU              Reviewed;         711 AA.
AC   P46344; P46345; P46346;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   11-DEC-2019, entry version 131.
DE   RecName: Full=Cyclic-di-AMP phosphodiesterase PgpH {ECO:0000303|PubMed:26240071};
DE            Short=c-di-AMP phosphodiesterase;
DE            EC=3.1.4.59 {ECO:0000250|UniProtKB:A0A0H3GGY3};
GN   Name=pgpH {ECO:0000303|PubMed:26240071}; Synonyms=yqfF;
GN   OrderedLocusNames=BSU25330;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ED40;
RA   Kim K., Hwang S., Suh J., Song B.-H., Hong S., Kim J.;
RT   "Nucleotide sequence upstream of the cdd locus in Bacillus subtilis.";
RL   Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   PROBABLE FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=26240071; DOI=10.1128/jb.00564-15;
RA   Gundlach J., Mehne F.M., Herzberg C., Kampf J., Valerius O., Kaever V.,
RA   Stuelke J.;
RT   "An essential poison: synthesis and degradation of cyclic di-AMP in
RT   Bacillus subtilis.";
RL   J. Bacteriol. 197:3265-3274(2015).
CC   -!- FUNCTION: Probably has phosphodiesterase (PDE) activity against cyclic-
CC       di-AMP (c-di-AMP); may be the major c-di-AMP PDE in the cell
CC       (PubMed:26240071). In B.subtilis c-di-AMP is a second messenger that
CC       mediates growth, DNA repair and cell wall homeostasis; it is toxic when
CC       present in excess (PubMed:26240071). {ECO:0000269|PubMed:26240071}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3',3'-c-di-AMP + H2O = 5'-O-phosphonoadenylyl-(3'->5')-
CC         adenosine + H(+); Xref=Rhea:RHEA:54420, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:71500, ChEBI:CHEBI:138171;
CC         EC=3.1.4.59; Evidence={ECO:0000250|UniProtKB:A0A0H3GGY3};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:A0A0H3GGY3};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: In strain 168 grown in minimal medium and
CC       glutamate, 3.5-fold increase in c-di-AMP levels, while a double pgpH-
CC       gdpP mutant has 4.2-fold increased levels of in c-di-AMP; double
CC       mutants die on solid medium after 2 days (PubMed:26240071).
CC       {ECO:0000269|PubMed:26240071}.
CC   -!- SIMILARITY: Belongs to the PgpH phosphodiesterase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA70040.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAA70041.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAA70042.1; Type=Frameshift; Evidence={ECO:0000305};
DR   EMBL; D84432; BAA12478.1; -; Genomic_DNA.
DR   EMBL; U29177; AAA70040.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U29177; AAA70041.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U29177; AAA70042.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL009126; CAB14462.1; -; Genomic_DNA.
DR   PIR; E69953; E69953.
DR   RefSeq; NP_390411.1; NC_000964.3.
DR   RefSeq; WP_010886570.1; NZ_JNCM01000036.1.
DR   SMR; P46344; -.
DR   IntAct; P46344; 38.
DR   STRING; 224308.BSU25330; -.
DR   jPOST; P46344; -.
DR   PaxDb; P46344; -.
DR   PRIDE; P46344; -.
DR   EnsemblBacteria; CAB14462; CAB14462; BSU25330.
DR   GeneID; 937877; -.
DR   KEGG; bsu:BSU25330; -.
DR   PATRIC; fig|224308.43.peg.2641; -.
DR   eggNOG; ENOG4105CTJ; Bacteria.
DR   eggNOG; COG1480; LUCA.
DR   HOGENOM; HOG000014932; -.
DR   InParanoid; P46344; -.
DR   KO; K07037; -.
DR   OMA; DFIRTHH; -.
DR   PhylomeDB; P46344; -.
DR   BioCyc; BSUB:BSU25330-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00077; HDc; 1.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR006675; HDIG_dom.
DR   InterPro; IPR011624; Metal-dep_PHydrolase_7TM_extra.
DR   InterPro; IPR011621; Metal-dep_PHydrolase_7TM_intra.
DR   Pfam; PF07698; 7TM-7TMR_HD; 1.
DR   Pfam; PF07697; 7TMR-HDED; 1.
DR   Pfam; PF01966; HD; 1.
DR   SMART; SM00471; HDc; 1.
DR   TIGRFAMs; TIGR00277; HDIG; 1.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
DR   PRODOM; P46344.
DR   SWISS-2DPAGE; P46344.
KW   Cell membrane; Hydrolase; Manganese; Membrane; Metal-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..711
FT                   /note="Cyclic-di-AMP phosphodiesterase PgpH"
FT                   /id="PRO_0000049797"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        311..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        336..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        360..380
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        384..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        413..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        448..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          501..643
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   METAL           504
FT                   /note="Manganese 1; via tele nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0H3GGY3"
FT   METAL           533
FT                   /note="Manganese 1; via tele nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0H3GGY3"
FT   METAL           534
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0H3GGY3"
FT   METAL           534
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0H3GGY3"
FT   METAL           570
FT                   /note="Manganese 2; via tele nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0H3GGY3"
FT   METAL           594
FT                   /note="Manganese 2; via tele nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0H3GGY3"
FT   METAL           595
FT                   /note="Manganese 2; via tele nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0H3GGY3"
FT   METAL           638
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0H3GGY3"
FT   BINDING         504
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0H3GGY3"
FT   BINDING         621
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0H3GGY3"
FT   BINDING         638
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0H3GGY3"
SQ   SEQUENCE   711 AA;  79167 MW;  1E424AB385D6E3B4 CRC64;
     MLKKKAKTKS SSKKWSSFKN ARSMHVLLYL LLAAIMFALL FVHVKPETLD LDLFSVSDKT
     IYAPATVEDQ KATEEKKQAA EDAVEDQYTL KKEYTDNRID LVSSIFDSIS EVKKSSEEGS
     KSPSEKSMVK SVKDKLTSDV NDSISEDSIK TLLKADSEDF SFVRDTVITA VNTVMSSEIP
     SDKLSDAKDK VEKELKSNSI PSKYLGAATE IGRFAIIPNY VFDPKATEAK RQEASDNVQQ
     VQIKQGQVLV EENDLIDREV YRKLELTGLL NNSNLFKPIS GLLIMIGLFI ATLVYYFEKQ
     KQNLKFKNQS ILLFSIITTL LLVIMEVVSL FQKMEYNNIG YLVPIAAGAI LIKLLMNERI
     AILGSIILAI CGSMMFNQGV TGTFNYVIGI YYLISGISGV LFLGKHNARS KILQTGLFVA
     FINMVVVLSL LLIQNTALSG LEIGTLMLMG VVSGFASSVL IIGLMPFFET GFGILSTMRL
     LELSNPNHPL LRKILTETPG TYHHSVMVAN LSEAACEAVG ANGLLARVGA YYHDLGKTKR
     PQYFIENQMN IDNPHDKLSP QLSKNIIISH TTDGANMLRS YKFPKELVDI AEQHHGTSLL
     KFFYYKAKEK GDQITEEEFR YPGPKPQSKE AAIISVADSV EAAVRSMHNP NPERIEKLVR
     GIISDKLQDG QFSECDLTFK ELDTIAKTLC ATLKGIFHSR IEYPEATKKV K
//

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