ID D1PYY4_9BACT Unreviewed; 474 AA.
AC D1PYY4;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Cardiolipin synthase {ECO:0000256|HAMAP-Rule:MF_01916};
DE Short=CL synthase {ECO:0000256|HAMAP-Rule:MF_01916};
DE EC=2.7.8.- {ECO:0000256|HAMAP-Rule:MF_01916};
GN Name=cls {ECO:0000313|EMBL:EFA43400.1};
GN ORFNames=HMPREF0645_2169 {ECO:0000313|EMBL:EFA43400.1};
OS Hallella bergensis DSM 17361.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hallella.
OX NCBI_TaxID=585502 {ECO:0000313|EMBL:EFA43400.1, ECO:0000313|Proteomes:UP000003160};
RN [1] {ECO:0000313|EMBL:EFA43400.1, ECO:0000313|Proteomes:UP000003160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17361 {ECO:0000313|EMBL:EFA43400.1,
RC ECO:0000313|Proteomes:UP000003160};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible phosphatidyl group transfer from one
CC phosphatidylglycerol molecule to another to form cardiolipin (CL)
CC (diphosphatidylglycerol) and glycerol. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01916};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01916};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01916}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01916}.
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:EFA43400.1}.
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DR EMBL; ACKS01000081; EFA43400.1; -; Genomic_DNA.
DR RefSeq; WP_007174272.1; NZ_GG704781.1.
DR AlphaFoldDB; D1PYY4; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_038053_1_2_10; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000003160; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008808; F:cardiolipin synthase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:InterPro.
DR CDD; cd09110; PLDc_CLS_1; 1.
DR CDD; cd09112; PLDc_CLS_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
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 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 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01916}; Hydrolase {ECO:0000313|EMBL:EFA43400.1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_01916};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_01916};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01916};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW ECO:0000256|HAMAP-Rule:MF_01916};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW Rule:MF_01916}; Reference proteome {ECO:0000313|Proteomes:UP000003160};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01916};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01916};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01916}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT DOMAIN 209..236
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 386..413
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 214
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 216
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 221
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 391
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 393
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 398
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ SEQUENCE 474 AA; 54941 MW; E3F911CACFE9F868 CRC64;
MTYMHWGWGV IYGLIVVGVM IKVLLDNRQP AKTMAWILVL WFLPLFGLIL YIFFGQNTRK
ERMISQGSLD QLTKRSMTGF VEQQNLRLPK SHQPLMHLFK NQNMALPFKN SEVEIFTDGY
QFFPALLYEI LKAQHHIHLL SYIFNDDELG NLVADALIDK AREGVEVRVI YDDVGCWRVS
GSFFERMRNG GVDVHAFMPV KFPAFTSKVN YRNHRKLIVI DGQVGFIGGF NIATRYVKGT
KKQKWRDTHL LVRGGAVYGI QRAFLVDWYF VDRTLITSRA YYPEQDSRIN NNCLAQVVTS
SPISPWPDIM QGYVRVLFEA RRYVYMESPY FLPKEPVMFA LRTAALTGVD VRLMIPKRGD
SRIVEWASTS YVMETIGAGV KVYLYKDGFN HSKLLVSDDC ISTCGSTNID ARSFEHNFES
NIFFYDEAMA LRMKKVFLDD MQHCVLIDEI RKVKNRSFLR RLWESVLRVV SPLL
//
