ID Q8G696_BIFLO Unreviewed; 205 AA.
AC Q8G696;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Possible CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyl-transferase {ECO:0000313|EMBL:AAN24567.1};
GN Name=pgsA {ECO:0000313|EMBL:AAN24567.1};
GN OrderedLocusNames=BL0750 {ECO:0000313|EMBL:AAN24567.1};
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=206672 {ECO:0000313|EMBL:AAN24567.1, ECO:0000313|Proteomes:UP000000439};
RN [1] {ECO:0000313|EMBL:AAN24567.1, ECO:0000313|Proteomes:UP000000439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705 {ECO:0000313|Proteomes:UP000000439};
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000256|ARBA:ARBA00005074}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000256|ARBA:ARBA00010441, ECO:0000256|RuleBase:RU003750}.
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DR EMBL; AE014295; AAN24567.1; -; Genomic_DNA.
DR RefSeq; NP_695931.1; NC_004307.2.
DR RefSeq; WP_007052288.1; NC_004307.2.
DR AlphaFoldDB; Q8G696; -.
DR STRING; 206672.BL0750; -.
DR EnsemblBacteria; AAN24567; AAN24567; BL0750.
DR KEGG; blo:BL0750; -.
DR PATRIC; fig|206672.9.peg.449; -.
DR HOGENOM; CLU_051314_6_1_11; -.
DR OrthoDB; 9796672at2; -.
DR PhylomeDB; Q8G696; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000000439; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.1760; -; 1.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS.
DR InterPro; IPR004570; Phosphatidylglycerol_P_synth.
DR PANTHER; PTHR14269:SF63; CARDIOLIPIN SYNTHASE-RELATED; 1.
DR PANTHER; PTHR14269; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE-RELATED; 1.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR PIRSF; PIRSF000847; Phos_ph_gly_syn; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Reference proteome {ECO:0000313|Proteomes:UP000000439};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003750};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 205 AA; 22670 MW; 85032F72F37877DA CRC64;
MTNQKVNTRY SPEARDIYFT VPNLISALRI ISIPFISVLI SKHEMIAALA LIAISSASDG
LDGIIARRFN QVSKIGQILD PIADRLLIFC SILALSVAGI IPWWMLIIVG LRDLWMAIQV
LWLAQYGYGP LPVHFVGKAG TALLMISIVS LIFADLGTNT FFHLLYIAAL AAGIWGIAMY
WLAGYIYTEQ GIRLLRKELG EKYGA
//
