ID M1N0R3_9CORY Unreviewed; 493 AA.
AC M1N0R3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Cardiolipin synthase {ECO:0000313|EMBL:AGF73489.1};
GN ORFNames=A605_12465 {ECO:0000313|EMBL:AGF73489.1};
OS Corynebacterium halotolerans YIM 70093 = DSM 44683.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1121362 {ECO:0000313|EMBL:AGF73489.1, ECO:0000313|Proteomes:UP000011723};
RN [1] {ECO:0000313|EMBL:AGF73489.1, ECO:0000313|Proteomes:UP000011723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 70093 {ECO:0000313|EMBL:AGF73489.1};
RX PubMed=23408721;
RA Ruckert C., Albersmeier A., Al-Dilaimi A., Niehaus K., Szczepanowski R.,
RA Kalinowski J.;
RT "Genome sequence of the halotolerant bacterium Corynebacterium halotolerans
RT type strain YIM 70093(T) (= DSM 44683(T)).";
RL Stand. Genomic Sci. 7:284-293(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP003697; AGF73489.1; -; Genomic_DNA.
DR RefSeq; WP_015401904.1; NZ_JIAJ01000006.1.
DR AlphaFoldDB; M1N0R3; -.
DR STRING; 1121362.A605_12465; -.
DR KEGG; chn:A605_12465; -.
DR PATRIC; fig|1121362.3.peg.2532; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_038053_1_0_11; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000011723; Chromosome.
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 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:UP000011723};
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 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 41..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 219..246
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 400..433
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 493 AA; 56280 MW; E59A4653ABC78A2B CRC64;
MSLSLDLSTW QFIGLLIDYT IKILAIGFVP EGRRPSSSTA WLLAILLLPY VGLPLFLLMG
SPYINRRRHR IQQEANVMIE DVHSHIPDQP RGMDLNPTVE STIRLNRRLT NLPAVYAHNL
GLHNDYNQAI RRMAEAIDEA REYVSVEIYI MAWDDTTEVF FHALERAVQR GVKVRLLFDQ
VGSWKYPGYL KLGRRLTRIG VDWHLMLPLK PWRARFRRPD LRNHRKLVIV DGEIGFMGSL
NLIDRSYLLR GHRRAGRKWV DSLVELSGPV VASLELVFAV DWYTESGETI DLAPPAVDTG
GTENTNIVQF VPSGPGYTTE PNLRMFNSII HHAKERLMLC SPYFIPDEAL LDAVTTACYR
GVRVELLVSE QSDQFMVHHA QSSYYQALLE AGVHIYLFPS PYVLHTKFML ADPDGEGDQA
VGAYGSANMD IRSFGLNYES TMMIAHGNLL DQLNELGGIY RSVSRQLTLE EWNRRGFFRR
YIDNVMKLTS ALQ
//