PGPB_BACSU
ID PGPB_BACSU Reviewed; 203 AA.
AC O34349; Q796B5;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Phosphatidylglycerophosphatase B {ECO:0000303|PubMed:28168443};
DE EC=3.1.3.27 {ECO:0000269|PubMed:28168443};
GN Name=pgpB {ECO:0000303|PubMed:28168443}; Synonyms=yodM;
GN OrderedLocusNames=BSU19650;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9734814; DOI=10.1093/dnares/5.3.195;
RA Ghim S.-Y., Choi S.-K., Shin B.-S., Jeong Y.-M., Sorokin A., Ehrlich S.D.,
RA Park S.-H.;
RT "Sequence analysis of the Bacillus subtilis 168 chromosome region between
RT the sspC and odhA loci (184 degrees-180 degrees).";
RL DNA Res. 5:195-201(1998).
RN [2]
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 [3]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-203, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=28168443; DOI=10.1007/s00018-017-2464-6;
RA Ghachi M.E., Howe N., Auger R., Lambion A., Guiseppi A., Delbrassine F.,
RA Manat G., Roure S., Peslier S., Sauvage E., Vogeley L.,
RA Rengifo-Gonzalez J.C., Charlier P., Mengin-Lecreulx D., Foglino M.,
RA Touze T., Caffrey M., Kerff F.;
RT "Crystal structure and biochemical characterization of the transmembrane
RT PAP2 type phosphatidylglycerol phosphate phosphatase from Bacillus
RT subtilis.";
RL Cell. Mol. Life Sci. 74:2319-2332(2017).
CC -!- FUNCTION: Catalyzes the dephosphorylation of
CC phosphatidylglycerophosphate (PGP) to phosphatidylglycerol. Also has
CC undecaprenyl pyrophosphate phosphatase activity, required for the
CC biosynthesis of the lipid carrier undecaprenyl phosphate.
CC {ECO:0000269|PubMed:28168443}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) +
CC H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphate;
CC Xref=Rhea:RHEA:33751, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:60110, ChEBI:CHEBI:64716; EC=3.1.3.27;
CC Evidence={ECO:0000269|PubMed:28168443};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
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DR EMBL; AF015775; AAB72067.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13856.1; -; Genomic_DNA.
DR PIR; H69903; H69903.
DR RefSeq; NP_389846.1; NC_000964.3.
DR RefSeq; WP_004399336.1; NZ_JNCM01000036.1.
DR PDB; 5JKI; X-ray; 2.25 A; A=1-203.
DR PDB; 6FMX; X-ray; 1.79 A; A=1-203.
DR PDBsum; 5JKI; -.
DR PDBsum; 6FMX; -.
DR AlphaFoldDB; O34349; -.
DR SMR; O34349; -.
DR STRING; 224308.BSU19650; -.
DR TCDB; 9.B.105.2.3; the lead resistance fusion protein (pbrbc) family.
DR PaxDb; O34349; -.
DR EnsemblBacteria; CAB13856; CAB13856; BSU_19650.
DR GeneID; 940034; -.
DR KEGG; bsu:BSU19650; -.
DR PATRIC; fig|224308.179.peg.2150; -.
DR eggNOG; COG0671; Bacteria.
DR InParanoid; O34349; -.
DR OMA; VIWLWCK; -.
DR PhylomeDB; O34349; -.
DR BioCyc; BSUB:BSU19650-MON; -.
DR BRENDA; 3.1.3.27; 658.
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:0008962; F:phosphatidylglycerophosphatase activity; IEA:UniProtKB-EC.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Hydrolase; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..203
FT /note="Phosphatidylglycerophosphatase B"
FT /id="PRO_0000359942"
FT TOPO_DOM 1
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:28168443"
FT TRANSMEM 2..17
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28168443"
FT TOPO_DOM 18..55
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:28168443"
FT TRANSMEM 56..74
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28168443"
FT TOPO_DOM 75..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:28168443"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28168443"
FT TOPO_DOM 100..119
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:28168443"
FT TRANSMEM 120..139
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28168443"
FT TOPO_DOM 140..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:28168443"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28168443"
FT TOPO_DOM 168..172
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:28168443"
FT TRANSMEM 173..196
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28168443"
FT TOPO_DOM 197..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:28168443"
FT REGION 96..104
FT /note="Phosphatase sequence motif I"
FT /evidence="ECO:0000305"
FT REGION 118..121
FT /note="Phosphatase sequence motif II"
FT /evidence="ECO:0000305"
FT REGION 164..175
FT /note="Phosphatase sequence motif III"
FT /evidence="ECO:0000305"
FT ACT_SITE 121
FT /note="Proton donors"
FT /evidence="ECO:0000305|PubMed:28168443"
FT ACT_SITE 171
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:28168443"
FT SITE 175
FT /note="Stabilizes the active site histidine for
FT nucleophilic attack"
FT /evidence="ECO:0000305|PubMed:28168443"
FT HELIX 2..17
FT /evidence="ECO:0007829|PDB:6FMX"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:6FMX"
FT HELIX 40..51
FT /evidence="ECO:0007829|PDB:6FMX"
FT HELIX 55..73
FT /evidence="ECO:0007829|PDB:6FMX"
FT HELIX 77..99
FT /evidence="ECO:0007829|PDB:6FMX"
FT HELIX 120..139
FT /evidence="ECO:0007829|PDB:6FMX"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:6FMX"
FT HELIX 147..167
FT /evidence="ECO:0007829|PDB:6FMX"
FT HELIX 173..196
FT /evidence="ECO:0007829|PDB:6FMX"
SQ SEQUENCE 203 AA; 22789 MW; 7C08E51810C20A56 CRC64;
MYKPVSLFLF FLILAAAIHT NAVQSADEAI SKAAVLIRQP WLNEVMTGIT HLGASSFLLP
LIVIIGAGMF FYRKTWDGLL MLLVFGTDRL LNKVLKEWIE RVRPDFAPLV HESSFSFPSG
HSMNAACVYP VIAYFLVKHL PFLSKHKKMV YIIAGVIAVL VGISRVYLGV HFVTDVLGGF
SLGLLLFFLV KGFDEKIKRF RQK
