ID   A0A2S5W1P8_9MICO        Unreviewed;       485 AA.
AC   A0A2S5W1P8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Cardiolipin synthase {ECO:0000313|EMBL:PPF80582.1};
GN   Name=cls {ECO:0000313|EMBL:PPF80582.1};
GN   ORFNames=C5B96_10840 {ECO:0000313|EMBL:PPF80582.1};
OS   Subtercola sp. Z020.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Subtercola.
OX   NCBI_TaxID=2080582 {ECO:0000313|EMBL:PPF80582.1, ECO:0000313|Proteomes:UP000238959};
RN   [1] {ECO:0000313|EMBL:PPF80582.1, ECO:0000313|Proteomes:UP000238959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z020 {ECO:0000313|EMBL:PPF80582.1,
RC   ECO:0000313|Proteomes:UP000238959};
RA   Davis E.W.II., Tabima J.F., Weisberg A.J., Lopes L.D., Wiseman M.S.,
RA   Wiseman M.S., Pupko T., Belcher M.S., Sechler A.J., Tancos M.A.,
RA   Schroeder B.K., Murray T.D., Luster D.G., Schneider W.L., Rogers E.,
RA   Andreote F.D., Grunwald N.J., Putnam M.L., Chang J.H.;
RT   "Bacteriophage NCPPB3778 and a type I-E CRISPR drive the evolution of the
RT   US Biological Select Agent, Rathayibacter toxicus.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PPF80582.1}.
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DR   EMBL; PSTT01000081; PPF80582.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S5W1P8; -.
DR   OrthoDB; 9762009at2; -.
DR   Proteomes; UP000238959; 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   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        36..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          214..241
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          398..425
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   485 AA;  55278 MW;  78A8045706AA4BAF CRC64;
     MVEIIIIVLF VIDFGVRVTA IIVVPRNRRP SSAMAWLLAI FLIPYIGVVV FLIIGSYKLP
     KKRREKQQAI NDFIIETTEG IDQVSNDHPW PAWLRSVVEL NRNLGAMPLV GGNKARLIGD
     YSQSIAEMTA DINQATKFVH CEFYIMSYDS VTAEFFLALE NAVKRGVIVR VLLDHIASLR
     SPGHRKTFRK LKQIGVSWHF MLPVQPLRGR WQRPDLRNHR KVLVVDGRVA YMGSQNLIDR
     SYNKRVNRRR GLQWQDLMTR VQGPIVNGIN AIFITDWYSE TNELLVRETE AITPGVVYES
     DDALDCQVVP SGPGFDGENN LRLFLALLYY AQKKIIITSP YFVPDDSMLY AITTASQRGV
     EVQLFVSEIG DQALVYHAQR SYYEALLRAG VQIWMYKAPY ILHAKHFTID DDVAVMGSSN
     MDIRSFQLNM EVSMMVRGAA FVTQMRAIED GYRASSRELT LAEWERQPLR STVLDNLARL
     TSGLQ
//