CLS2_STAES
ID CLS2_STAES Reviewed; 488 AA.
AC Q8CNK3;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Cardiolipin synthase 2 {ECO:0000255|HAMAP-Rule:MF_01916};
DE Short=CL synthase 2 {ECO:0000255|HAMAP-Rule:MF_01916};
DE EC=2.7.8.- {ECO:0000255|HAMAP-Rule:MF_01916};
GN Name=cls2; OrderedLocusNames=SE_1687;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
CC -!- FUNCTION: Catalyzes the reversible phosphatidyl group transfer from one
CC phosphatidylglycerol molecule to another to form cardiolipin (CL)
CC (diphosphatidylglycerol) and glycerol. {ECO:0000255|HAMAP-
CC Rule:MF_01916}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a
CC cardiolipin + glycerol; Xref=Rhea:RHEA:31451, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:62237, ChEBI:CHEBI:64716; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01916};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01916};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01916}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01916}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO05286.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE015929; AAO05286.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_765242.1; NC_004461.1.
DR AlphaFoldDB; Q8CNK3; -.
DR SMR; Q8CNK3; -.
DR STRING; 176280.SE_1687; -.
DR DNASU; 1057231; -.
DR EnsemblBacteria; AAO05286; AAO05286; SE_1687.
DR KEGG; sep:SE_1687; -.
DR PATRIC; fig|176280.10.peg.1647; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_038053_1_1_9; -.
DR Proteomes; UP000001411; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008808; F:cardiolipin synthase activity; IEA:InterPro.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:InterPro.
DR HAMAP; MF_01916; Cardiolipin_synth_Cls; 1.
DR InterPro; IPR030874; Cardiolipin_synth_Firmi.
DR InterPro; IPR022924; Cardiolipin_synthase.
DR InterPro; IPR027379; CLS_N.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR Pfam; PF13091; PLDc_2; 2.
DR Pfam; PF13396; PLDc_N; 1.
DR SMART; SM00155; PLDc; 2.
DR TIGRFAMs; TIGR04265; bac_cardiolipin; 1.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Cell membrane; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Repeat; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..488
FT /note="Cardiolipin synthase 2"
FT /id="PRO_0000201276"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT DOMAIN 223..250
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT DOMAIN 401..428
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 228
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 230
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 235
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 406
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 408
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 413
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
SQ SEQUENCE 488 AA; 56016 MW; 4CFA4E7CE4041E86 CRC64;
MALHQSNIII NILLVSAFLL NLVFAFIIIF MERRTANSIW AWLLVLVFLP LVGFILYLLL
GRQIQREHIF KLAKEDKVGL EMIVDEQLEA LKKQDFSKGN HQIVKFKEMV QMLLYNNAAF
LTTDNDLTIY TDGHQKFDDL INDIRHAQSY IHIQYYIIHS DNLGKQLLHE LEKKAEEGIE
VKMLYDDMGS RDLRKKDLKK FRQKGGHAES FFPSKLPLIN LRMNNRNHRK IVVIDGTIGY
VGGFNVGDEY IGKSKKFGYW RDTHLRIKGD AVNALQLRFI LDWNSQSTRD NLTYESRYFP
DVDSGGTIGI QIASSGPDED WEQIKYGYLK MISSAKESIY IQSPYFIPDQ AFLDSIKIAA
LGGVDVNIMV PNKRDHPFVY WATLKNVASL LEAGVNVYHY DNGFLHSKTL VIDDEVASVG
TANMDNRSFT LNFEVNAFIY DEGVARSLKQ AFINDMKLSN KLTSEEYAKR NLLVKFKEGI
SQLLSPIL
