ID M1TS65_9CORY Unreviewed; 212 AA.
AC M1TS65;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 1-phosphatidyltransferase {ECO:0000256|ARBA:ARBA00013170};
DE EC=2.7.8.5 {ECO:0000256|ARBA:ARBA00013170};
GN ORFNames=H924_08245 {ECO:0000313|EMBL:AGG67091.1};
OS Corynebacterium callunae DSM 20147.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1121353 {ECO:0000313|EMBL:AGG67091.1, ECO:0000313|Proteomes:UP000011760};
RN [1] {ECO:0000313|EMBL:AGG67091.1, ECO:0000313|Proteomes:UP000011760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20147 {ECO:0000313|EMBL:AGG67091.1,
RC ECO:0000313|Proteomes:UP000011760};
RA Ruckert C., Albersmeier A., Kalinowski J.;
RT "The complete genome sequence of Corynebacterium callunae DSM 20147.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-
CC diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP +
CC H(+); Xref=Rhea:RHEA:12593, ChEBI:CHEBI:15378, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:60110, ChEBI:CHEBI:60377; EC=2.7.8.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001566};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000256|ARBA:ARBA00005074}.
CC -!- PATHWAY: Phospholipid metabolism. {ECO:0000256|ARBA:ARBA00025707}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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; CP004354; AGG67091.1; -; Genomic_DNA.
DR RefSeq; WP_015651522.1; NZ_ATVF01000003.1.
DR AlphaFoldDB; M1TS65; -.
DR STRING; 1121353.H924_08245; -.
DR KEGG; ccn:H924_08245; -.
DR PATRIC; fig|1121353.3.peg.1681; -.
DR eggNOG; COG0558; Bacteria.
DR HOGENOM; CLU_051314_2_0_11; -.
DR OrthoDB; 9796672at2; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000011760; 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 NCBIfam; TIGR00560; pgsA; 1.
DR PANTHER; PTHR14269:SF60; CARDIOLIPIN SYNTHASE (CMP-FORMING); 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 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 62..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 212 AA; 23269 MW; CBB3E4D640EE7FEE CRC64;
MNDASAGAHG AQDPQGTQKT QTGQSSSTQP SNWNLPNFLT SLRIIVIPLF AWLTLKGETE
NNAFAWWALI VFILLMITDK LDGDIARARG LVTNFGKIAD PIADKALMTT AFVSFNIIGS
LPWWVTILIV IREFGITIWR FFQLRNGNVV PASKGGKLKT VLQTVAVALY LCPLPSWMDI
PSQAVMYLAL IVTVVTGVQY LWDSRTAGQS AK
//
