ID CLS1_BACCR Reviewed; 509 AA.
AC Q81I00;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=Cardiolipin synthase 1 {ECO:0000255|HAMAP-Rule:MF_01916};
DE Short=CL synthase 1 {ECO:0000255|HAMAP-Rule:MF_01916};
DE EC=2.7.8.- {ECO:0000255|HAMAP-Rule:MF_01916};
GN Name=cls1; OrderedLocusNames=BC_0626;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(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}.
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DR EMBL; AE016877; AAP07643.1; -; Genomic_DNA.
DR RefSeq; NP_830442.1; NC_004722.1.
DR RefSeq; WP_000743034.1; NZ_CP034551.1.
DR AlphaFoldDB; Q81I00; -.
DR SMR; Q81I00; -.
DR STRING; 226900.BC_0626; -.
DR KEGG; bce:BC0626; -.
DR PATRIC; fig|226900.8.peg.585; -.
DR HOGENOM; CLU_038053_1_2_9; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000001417; Chromosome.
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 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:SF20; CARDIOLIPIN SYNTHASE YWIE-RELATED; 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; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Repeat; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..509
FT /note="Cardiolipin synthase 1"
FT /id="PRO_0000201243"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT DOMAIN 238..265
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT DOMAIN 422..449
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 243
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 245
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 250
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 427
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 429
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 434
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
SQ SEQUENCE 509 AA; 58193 MW; BC593C235250EEF9 CRC64;
MKKPIVQLLL IFTIVSIVLF LLNTSYISLY TFVGALWSIT IVGISFVIFI ENRSPQSTLA
WFLVLALLPI IGVLLYAIFG RSRWRRKKHL HRSEEQRKLF REILEGRRLE LLLTVPLNER
SIHLTEVIQK FGGGPAADRT TTKLLTNGDQ TFSEILRAIE QAKHHIHIQY YIYKSDEIGT
KVRDALIQKA KDGVIVRFLY DGLGSNTLRR RFLQPMKEAG IEIVEFDPIF SAWLLETVNY
RNHRKIVIVD GEIGFTGGLN VGDEYLGRSK KFPVWRDSHL KIEGKALYKL QAIFLEDWLY
ASSGLNTYSW DQFMNRQYFP GKEISNAEGA VQIVASGPSS DDKSIRNTLL AVMGSAKKSI
WIATPYFIPD QETLTLLRLS AIAGIDVRIL YPGKSDSIIS DQASQSYFTP LLKAGASIYS
YKDGFMHAKI VLVDDTIATI GTANMDVRSF ELNYEIISVL YESKTVHDIK RDFEEDFKHS
TEIKWNSFQK RSIKKRILES FMRLISPLL
//
