ID A0A1X6X342_9MICO Unreviewed; 495 AA.
AC A0A1X6X342;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Cardiolipin synthetase {ECO:0000313|EMBL:SLM92264.1};
DE EC=2.7.8.- {ECO:0000313|EMBL:SLM92264.1};
GN ORFNames=FM110_07790 {ECO:0000313|EMBL:SLM92264.1};
OS Brachybacterium nesterenkovii.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=47847 {ECO:0000313|EMBL:SLM92264.1, ECO:0000313|Proteomes:UP000195981};
RN [1] {ECO:0000313|EMBL:SLM92264.1, ECO:0000313|Proteomes:UP000195981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP104813 {ECO:0000313|EMBL:SLM92264.1,
RC ECO:0000313|Proteomes:UP000195981};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FWFG01000068; SLM92264.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6X342; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000195981; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0008808; F:cardiolipin synthase activity; IEA:InterPro.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:InterPro.
DR CDD; cd09158; PLDc_EcCLS_like_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR InterPro; IPR022924; Cardiolipin_synthase.
DR InterPro; IPR027379; CLS_N.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR NCBIfam; TIGR04265; bac_cardiolipin; 1.
DR PANTHER; PTHR21248; CARDIOLIPIN SYNTHASE; 1.
DR PANTHER; PTHR21248:SF22; PHOSPHOLIPASE D; 1.
DR Pfam; PF13091; PLDc_2; 2.
DR Pfam; PF13396; PLDc_N; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:UP000195981};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SLM92264.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 227..254
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 408..435
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 495 AA; 56403 MW; 548D030FB76E42B5 CRC64;
MDSMWAWIVA HWPVASTTLY TLVDVVLRLV AIVVVPRNRR PASAIAWLLA IMALPIVGFP
LYLMLGKAQL PRRRREKQRV VNRLMRGRAQ DIPDSELDDD SPSWLQSAVQ LNRELGAYPL
TGNNSADLET DYERTLARMA ADIRSARDSV HALFYTMGLD EVTEDFFAAL GEAAERGVTV
RVLYDHFGSA THRRVYRAMK HHLDACGIEH YPMMPIKPFH DGALQRPDLR NHRKVLVVDG
EVAWMGSQNI IARHYDKRAN IRRGLRWQET MVRLRGPIVS ELNLLFATDW FFESDEFLAE
SELVRHSPDT SGSFECQILP SGPGFVLENN LLLFNQLFYS ARERIVAVSP YFVPDETMHA
ALITAAKRGV QVQLLVSKAA DQFIVSHAQR SYYSPLLEAG VEIWEFEEPY ILHAKHITID
DSVTVIGSSN MDIRSFLLDM ESSLMIGGCD FIERMREIED GYRARSTRLD PSEWAQRSFP
RRTLDNLCRL ASAIV
//
