PCRB_BACSU
ID PCRB_BACSU Reviewed; 228 AA.
AC O34790;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Heptaprenylglyceryl phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00112, ECO:0000305};
DE Short=HepGP synthase {ECO:0000255|HAMAP-Rule:MF_00112, ECO:0000305};
DE EC=2.5.1.n9 {ECO:0000255|HAMAP-Rule:MF_00112, ECO:0000269|PubMed:21761520, ECO:0000269|PubMed:24684232};
DE AltName: Full=Glycerol-1-phosphate heptaprenyltransferase {ECO:0000255|HAMAP-Rule:MF_00112, ECO:0000305};
GN Name=pcrB {ECO:0000255|HAMAP-Rule:MF_00112}; Synonyms=yerE;
GN OrderedLocusNames=BSU06600;
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;
RX PubMed=9701819; DOI=10.1046/j.1365-2958.1998.00927.x;
RA Petit M.-A., Dervyn E., Rose M., Entian K.-D., McGovern S., Ehrlich S.D.,
RA Bruand C.;
RT "PcrA is an essential DNA helicase of Bacillus subtilis fulfilling
RT functions both in repair and rolling-circle replication.";
RL Mol. Microbiol. 29:261-273(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 PUTATIVE FUNCTION.
RC STRAIN=168;
RX PubMed=18558723; DOI=10.1021/bi8005779;
RA Guldan H., Sterner R., Babinger P.;
RT "Identification and characterization of a bacterial glycerol-1-phosphate
RT dehydrogenase: Ni(2+)-dependent AraM from Bacillus subtilis.";
RL Biochemistry 47:7376-7384(2008).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBUNIT, PATHWAY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=21761520; DOI=10.1002/anie.201101832;
RA Guldan H., Matysik F.M., Bocola M., Sterner R., Babinger P.;
RT "Functional assignment of an enzyme that catalyzes the synthesis of an
RT archaea-type ether lipid in bacteria.";
RL Angew. Chem. Int. Ed. Engl. 50:8188-8191(2011).
RN [5]
RP FUNCTION AS A PRENYLTRANSFERASE, STEREOCHEMISTRY, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=168 / PY79;
RX PubMed=21214173; DOI=10.1021/ja109578b;
RA Doud E.H., Perlstein D.L., Wolpert M., Cane D.E., Walker S.;
RT "Two distinct mechanisms for TIM barrel prenyltransferases in bacteria.";
RL J. Am. Chem. Soc. 133:1270-1273(2011).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=24684232; DOI=10.1111/mmi.12596;
RA Peterhoff D., Beer B., Rajendran C., Kumpula E.P., Kapetaniou E.,
RA Guldan H., Wierenga R.K., Sterner R., Babinger P.;
RT "A comprehensive analysis of the geranylgeranylglyceryl phosphate synthase
RT enzyme family identifies novel members and reveals mechanisms of substrate
RT specificity and quaternary structure organization.";
RL Mol. Microbiol. 92:885-899(2014).
RN [7] {ECO:0007744|PDB:1VIZ}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-228.
RX PubMed=16021622; DOI=10.1002/prot.20541;
RA Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., Bergseid M.G.,
RA Buchanan S.G., Buchanan M.D., Batiyenko Y., Christopher J.A., Emtage S.,
RA Eroshkina A., Feil I., Furlong E.B., Gajiwala K.S., Gao X., He D.,
RA Hendle J., Huber A., Hoda K., Kearins P., Kissinger C., Laubert B.,
RA Lewis H.A., Lin J., Loomis K., Lorimer D., Louie G., Maletic M.,
RA Marsh C.D., Miller I., Molinari J., Muller-Dieckmann H.J., Newman J.M.,
RA Noland B.W., Pagarigan B., Park F., Peat T.S., Post K.W., Radojicic S.,
RA Ramos A., Romero R., Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J.,
RA Winhoven J., Wright T.A., Wu L., Xu J., Harris T.J.R.;
RT "Structural analysis of a set of proteins resulting from a bacterial
RT genomics project.";
RL Proteins 60:787-796(2005).
RN [8] {ECO:0007744|PDB:3VZX, ECO:0007744|PDB:3VZY, ECO:0007744|PDB:3VZZ, ECO:0007744|PDB:3W00}
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) IN COMPLEX WITH GLYCEROL
RP 1-PHOSPHATE, AND SUBUNIT.
RX PubMed=23322418; DOI=10.1002/cbic.201200748;
RA Ren F., Feng X., Ko T.P., Huang C.H., Hu Y., Chan H.C., Liu Y.L., Wang K.,
RA Chen C.C., Pang X., He M., Li Y., Oldfield E., Guo R.T.;
RT "Insights into TIM-barrel prenyl transferase mechanisms: crystal structures
RT of PcrB from Bacillus subtilis and Staphylococcus aureus.";
RL ChemBioChem 14:195-199(2013).
CC -!- FUNCTION: Prenyltransferase that catalyzes in vivo the transfer of the
CC heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon
CC atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing
CC heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond-
CC formation step in the biosynthesis of archaea-type G1P-based membrane
CC lipids found in Bacillales. To a much lesser extent, is also able to
CC use geranyl diphosphate (GPP; C10) and geranylgeranyl diphosphate
CC (GGPP; C20) as the prenyl donors, but not farnesyl pyrophosphate (FPP;
CC C15). Cannot use glycerol-3-phosphate (G3P) or 3-phosphoglycerate (3PG)
CC as an acceptor. {ECO:0000269|PubMed:21214173,
CC ECO:0000269|PubMed:21761520, ECO:0000269|PubMed:24684232}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-heptaprenyl diphosphate + sn-glycerol 1-phosphate =
CC 3-heptaprenyl-sn-glycero-1-phosphate + diphosphate;
CC Xref=Rhea:RHEA:33495, ChEBI:CHEBI:33019, ChEBI:CHEBI:57685,
CC ChEBI:CHEBI:58206, ChEBI:CHEBI:64781; EC=2.5.1.n9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00112,
CC ECO:0000269|PubMed:21761520, ECO:0000269|PubMed:24684232};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00112};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_00112, ECO:0000269|PubMed:21761520}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00112,
CC ECO:0000269|PubMed:21761520, ECO:0000269|PubMed:23322418,
CC ECO:0000269|PubMed:24684232}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a cloggy growth and
CC do not produce the dephosphorylated and acetylated derivatives of
CC HepGP. {ECO:0000269|PubMed:21761520}.
CC -!- MISCELLANEOUS: The HepGP product, which is the first archaea-type G1P-
CC based ether lipid being identified within the phylogenetic domain of
CC the bacteria, was found to be subsequently dephosphorylated and
CC acetylated in vivo. However, HepG and its acetylated derivatives
CC represent only a minor fraction of the total lipid in B.subtilis.
CC -!- SIMILARITY: Belongs to the GGGP/HepGP synthase family. Group I
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00112}.
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DR EMBL; Y15254; CAA75551.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12480.1; -; Genomic_DNA.
DR PIR; D69794; D69794.
DR RefSeq; NP_388542.1; NC_000964.3.
DR RefSeq; WP_003233922.1; NZ_JNCM01000032.1.
DR PDB; 1VIZ; X-ray; 1.85 A; A/B=2-228.
DR PDB; 3VZX; X-ray; 1.54 A; A/B=1-228.
DR PDB; 3VZY; X-ray; 1.63 A; A/B=1-228.
DR PDB; 3VZZ; X-ray; 2.04 A; A/B=1-228.
DR PDB; 3W00; X-ray; 2.50 A; A/B=1-228.
DR PDBsum; 1VIZ; -.
DR PDBsum; 3VZX; -.
DR PDBsum; 3VZY; -.
DR PDBsum; 3VZZ; -.
DR PDBsum; 3W00; -.
DR AlphaFoldDB; O34790; -.
DR SMR; O34790; -.
DR STRING; 224308.BSU06600; -.
DR jPOST; O34790; -.
DR PaxDb; O34790; -.
DR PRIDE; O34790; -.
DR EnsemblBacteria; CAB12480; CAB12480; BSU_06600.
DR GeneID; 936052; -.
DR KEGG; bsu:BSU06600; -.
DR PATRIC; fig|224308.179.peg.718; -.
DR eggNOG; COG1646; Bacteria.
DR InParanoid; O34790; -.
DR OMA; TGAHKEW; -.
DR PhylomeDB; O34790; -.
DR BioCyc; BSUB:BSU06600-MON; -.
DR UniPathway; UPA00940; -.
DR EvolutionaryTrace; O34790; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0002094; F:polyprenyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IDA:UniProtKB.
DR CDD; cd02812; PcrB_like; 1.
DR Gene3D; 3.20.20.390; -; 1.
DR HAMAP; MF_00112; GGGP_HepGP_synthase; 1.
DR InterPro; IPR039074; GGGP/HepGP_synthase_I.
DR InterPro; IPR038597; GGGP/HepGP_synthase_sf.
DR InterPro; IPR008205; GGGP_HepGP_synthase.
DR PANTHER; PTHR40029; PTHR40029; 1.
DR Pfam; PF01884; PcrB; 1.
DR TIGRFAMs; TIGR01768; GGGP-family; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW Metal-binding; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase.
FT CHAIN 1..228
FT /note="Heptaprenylglyceryl phosphate synthase"
FT /id="PRO_0000138711"
FT BINDING 12
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112,
FT ECO:0000269|PubMed:23322418, ECO:0007744|PDB:3VZY,
FT ECO:0007744|PDB:3W00"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 158..163
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112,
FT ECO:0000269|PubMed:23322418, ECO:0007744|PDB:3VZY,
FT ECO:0007744|PDB:3W00"
FT BINDING 188
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112,
FT ECO:0000269|PubMed:23322418, ECO:0007744|PDB:3VZY,
FT ECO:0007744|PDB:3W00"
FT BINDING 208..209
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112,
FT ECO:0000269|PubMed:23322418, ECO:0007744|PDB:3VZY,
FT ECO:0007744|PDB:3W00"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:3VZX"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:3VZX"
FT HELIX 23..28
FT /evidence="ECO:0007829|PDB:3VZX"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:3VZX"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:3VZY"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:3VZX"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:3VZX"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:3VZX"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:3VZX"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:3VZX"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:3VZX"
FT TURN 90..94
FT /evidence="ECO:0007829|PDB:3VZX"
FT HELIX 95..110
FT /evidence="ECO:0007829|PDB:3VZX"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:3VZX"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:3VZX"
FT HELIX 126..130
FT /evidence="ECO:0007829|PDB:3VZX"
FT HELIX 139..151
FT /evidence="ECO:0007829|PDB:3VZX"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:3VZX"
FT HELIX 168..177
FT /evidence="ECO:0007829|PDB:3VZX"
FT STRAND 179..188
FT /evidence="ECO:0007829|PDB:3VZX"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:3VZX"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:3VZX"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:3VZX"
FT HELIX 215..219
FT /evidence="ECO:0007829|PDB:3VZX"
FT HELIX 221..226
FT /evidence="ECO:0007829|PDB:3VZX"
SQ SEQUENCE 228 AA; 25088 MW; 05360F1F863A5ABA CRC64;
MYDVTEWKHV FKLDPNKDLP DEQLEILCES GTDAVIIGGS DGVTEDNVLR MMSKVRRFLV
PCVLEVSAIE AIVPGFDLYF IPSVLNSKNA DWIVGMHQKA MKEYGELMSM EEIVAEGYCI
ANPDCKAAAL TEADADLNMD DIVAYARVSE LLQLPIFYLE YSGVLGDIEA VKKTKAVLET
STLFYGGGIK DAETAKQYAE HADVIVVGNA VYEDFDRALK TVAAVKGE
