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Database: UniProt
Entry: D4YUY9_9LACO
LinkDB: D4YUY9_9LACO
Original site: D4YUY9_9LACO 
ID   D4YUY9_9LACO            Unreviewed;       485 AA.
AC   D4YUY9;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   24-JAN-2024, entry version 70.
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=cls2 {ECO:0000313|EMBL:EFG55040.1};
GN   ORFNames=HMPREF0493_1350 {ECO:0000313|EMBL:EFG55040.1};
OS   Lactobacillus amylolyticus DSM 11664.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=585524 {ECO:0000313|EMBL:EFG55040.1, ECO:0000313|Proteomes:UP000004069};
RN   [1] {ECO:0000313|EMBL:EFG55040.1, ECO:0000313|Proteomes:UP000004069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11664 {ECO:0000313|EMBL:EFG55040.1,
RC   ECO:0000313|Proteomes:UP000004069};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (APR-2010) 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:EFG55040.1}.
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DR   EMBL; ADNY01000055; EFG55040.1; -; Genomic_DNA.
DR   RefSeq; WP_006352499.1; NZ_AZEP01000009.1.
DR   AlphaFoldDB; D4YUY9; -.
DR   STRING; 83683.B1745_00630; -.
DR   PATRIC; fig|585524.9.peg.1637; -.
DR   eggNOG; COG1502; Bacteria.
DR   OrthoDB; 9762009at2; -.
DR   Proteomes; UP000004069; 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:EFG55040.1};
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:UP000004069};
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..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   TRANSMEM        36..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   DOMAIN          214..241
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          398..425
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   ACT_SITE        219
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   ACT_SITE        221
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   ACT_SITE        226
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   ACT_SITE        403
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   ACT_SITE        405
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   ACT_SITE        410
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ   SEQUENCE   485 AA;  56663 MW;  2872A1EFC9E02EBD CRC64;
     MIWLHDLWRI IVITNTILAF YIVFHRRRSV STTWAWLIIL LVLPIIGLIL YGFFGRGISQ
     ENIFAINRQK HLGLRNVQET ITKAPKKVSP DDTSTKGKIA IKYFNKDHNS PLTKNNHVDL
     YNDGHAMFKD MIRDIEKAKK TVNVEFYTFY NDEIGNRMLN LLIKKAKSGV KVNVLYDAWG
     SMGATKAWFN QLRKAGGEVL PFITSRNMIT RYRINYHLHR KIVVIDGKIS WTGGFNIGDQ
     YLGKKKKLGY WRDSQVRIVG SASLLLQERF VMDWNASIYK NTQVITYSDL YFPDFDENDI
     ENGDVATQVV FDGPDRYEQY MRNGMMRLML MARKRLWIQT PYLIPDDAMF AAWQTIASSG
     IDVRIMIPCK PDHPFIYRAT QWYANELTHY GIKVYIYNHG FIHAKTTVID DLYSSVGSMN
     QDYRSYDLNF EDNVIFYDKK FNKKMTDTFE KDMEDSTLLT KEMIAKQSRP LKTLQSFSRM
     LSPIL
//
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