ID A0A0Q4UX27_9MICO Unreviewed; 486 AA.
AC A0A0Q4UX27;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Cardiolipin synthase {ECO:0000313|EMBL:KQO62339.1};
GN ORFNames=ASF23_11150 {ECO:0000313|EMBL:KQO62339.1};
OS Curtobacterium sp. Leaf261.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1736311 {ECO:0000313|EMBL:KQO62339.1, ECO:0000313|Proteomes:UP000050821};
RN [1] {ECO:0000313|EMBL:KQO62339.1, ECO:0000313|Proteomes:UP000050821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf261 {ECO:0000313|EMBL:KQO62339.1,
RC ECO:0000313|Proteomes:UP000050821};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQO62339.1, ECO:0000313|Proteomes:UP000050821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf261 {ECO:0000313|EMBL:KQO62339.1,
RC ECO:0000313|Proteomes:UP000050821};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQO62339.1}.
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DR EMBL; LMMJ01000009; KQO62339.1; -; Genomic_DNA.
DR RefSeq; WP_055954036.1; NZ_LMMJ01000009.1.
DR AlphaFoldDB; A0A0Q4UX27; -.
DR STRING; 1736311.ASF23_11150; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000050821; 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:UP000050821};
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 37..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 218..245
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 399..426
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 486 AA; 55226 MW; 1C0E5D0D2DFB08F7 CRC64;
MEHWLGITIT VLLILLDLAI RAFSIIYVPI DRKPQTATGW LLAIFLIPYI GFIVFLIIGS
TKLPKARREK QSEINDYILD QTEGMDRVKT DETWPKWLNS VVQLNRGLGA MPLVGGNTAE
LYPDSVESIA AMTRAVDEAE RFVHVEFYIA TIDPTTKPFF DALERAVERG VSVKFLMDHI
ASRGYPGYKA TKARLDDMGA EWHLMLPILP LQGKFQRPDL RNHRKILVVD GRVGFTGSQN
LIDDSYDVKA HVEKGLRYKD LMARFEGPIV AGINALFITD WYSETDELLR EREPVQRAEP
HPEMLDAQVV PSGPGFDGEN NLRLFNALLY AAQDRVSITS PYFVPDESML YAITTTAQRG
VAVELFVGEI GDHTMTWHAQ RSYYEALLRA GVRIFLYKQP TILHAKHFTI DDSVSVIGSS
NMDMRSFSLN LEITVMVRGR KFVDQLRQVQ DDYRAESFEI TLDEWVQRPT RSQVLDNVAR
LTAALQ
//
