ID H6N545_GORPV Unreviewed; 214 AA.
AC H6N545;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=CDP-alcohol phosphatidyltransferase Pgs {ECO:0000313|EMBL:AFA76090.1};
DE EC=2.7.8.- {ECO:0000313|EMBL:AFA76090.1};
GN Name=pgs {ECO:0000313|EMBL:AFA76090.1};
GN OrderedLocusNames=GPOL_174p00710 {ECO:0000313|EMBL:AFA76090.1};
OS Gordonia polyisoprenivorans (strain DSM 44266 / VH2).
OG Plasmid p174 {ECO:0000313|EMBL:AFA76090.1,
OG ECO:0000313|Proteomes:UP000009154}.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA76090.1, ECO:0000313|Proteomes:UP000009154};
RN [1] {ECO:0000313|EMBL:AFA76090.1, ECO:0000313|Proteomes:UP000009154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44266 / VH2 {ECO:0000313|Proteomes:UP000009154};
RC PLASMID=p174 {ECO:0000313|EMBL:AFA76090.1,
RC ECO:0000313|Proteomes:UP000009154};
RX PubMed=22327575; DOI=10.1128/AEM.07969-11;
RA Hiessl S., Schuldes J., Thurmer A., Halbsguth T., Broker D., Angelov A.,
RA Liebl W., Daniel R., Steinbuchel A.;
RT "Involvement of two latex-clearing proteins during rubber degradation and
RT insights into the subsequent degradation pathway revealed by the genome
RT sequence of Gordonia polyisoprenivorans strain VH2.";
RL Appl. Environ. Microbiol. 78:2874-2887(2012).
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; CP003120; AFA76090.1; -; Genomic_DNA.
DR RefSeq; WP_014362179.1; NC_016907.1.
DR AlphaFoldDB; H6N545; -.
DR KEGG; gpo:GPOL_174p00710; -.
DR eggNOG; COG0558; Bacteria.
DR HOGENOM; CLU_051314_6_1_11; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000009154; Plasmid p174.
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 Plasmid {ECO:0000313|EMBL:AFA76090.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009154};
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 28..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 52..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 214 AA; 23309 MW; A84A157163F3D012 CRC64;
MTGSGGDDDG PVTAAAPGAD RILTVPNALS VLRLVLIPVF IWLVIVEKAD GWAFVVLFVS
GVTDWLDGKL ARLLDQSSRL GELLDPAADR LYIVVIPICF GLRDFVPWWL IGIIIARDVL
LFASAPLLRS RGLVALPVLY VGKAATFALM SAFPWLLAGQ LDSVIGTICY PIGWAFLIWG
VGMYLWSFVL YWAQTIMVMR TMPRLDRVSS AAAG
//