ID A0A1H9AZ81_9FIRM Unreviewed; 566 AA.
AC A0A1H9AZ81;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Cardiolipin synthase {ECO:0000313|EMBL:SEP82044.1};
GN ORFNames=SAMN02910382_01115 {ECO:0000313|EMBL:SEP82044.1};
OS Butyrivibrio sp. TB.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1520809 {ECO:0000313|EMBL:SEP82044.1, ECO:0000313|Proteomes:UP000198682};
RN [1] {ECO:0000313|EMBL:SEP82044.1, ECO:0000313|Proteomes:UP000198682}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TB {ECO:0000313|EMBL:SEP82044.1,
RC ECO:0000313|Proteomes:UP000198682};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOER01000006; SEP82044.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9AZ81; -.
DR Proteomes; UP000198682; 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; cd09160; PLDc_SMU_988_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 65..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 121..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 297..324
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 479..506
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 566 AA; 64782 MW; F0B1D6BA2C26F4BF CRC64;
MYKDKGKEPI IKNQDNLNNK NDTNNKSDIN NKNKAHKKSL DESLKVKINP KGKANRNAQN
SVNRIAAIAI FTLLQIVVLG LMLYEFSNYS IYFQIGFGVL SIIIVLTIYG RHTNSANKMP
WMIFIMCVPV FGILLYLLMG RPGVTAKAKK RFEEIDSKIL PYLKPRRSIL NSLEISDPNI
ASRVKYVEDY GHFPVYKNTD VVYFDDARKG IEDQVRELEK ARSFIFMEYY AIQDTDTFEP
IKEVLARKAA EGLEVRVIYD DIGSGGFINS GFIKRMEDLG IKCRVFNHVS PFFQVIMNNR
DHRKITVIDG KVGYTGGYNI ADLYTHRIEP HGFWKDTGVR LTGDGVVTLT ALFLEMWNAV
KANDIDDNDL SIFFPRVSYT AVEKDCFVQP FADTPLDEEL LGENVYMGML QTARKYCWFV
TPYLVITDEL CREFEIAVKR GVDVRIITPG IPDKKVVYAI TRSYYNELAR NGVRIFEYTP
GFCHAKMCIA DGQCAAVGTL NLDFRSLYLH FEDGVYLYNC KAINDIEEDF KEMFKVSTEV
TDKYHSHRSV PLRISQCALR IVAPLV
//
