ID Q9I1W0_PSEAE Unreviewed; 401 AA.
AC Q9I1W0;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 24-JAN-2024, entry version 114.
DE RecName: Full=Cardiolipin synthase B {ECO:0000256|HAMAP-Rule:MF_01917};
DE Short=CL synthase {ECO:0000256|HAMAP-Rule:MF_01917};
DE EC=2.7.8.- {ECO:0000256|HAMAP-Rule:MF_01917};
GN Name=clsB {ECO:0000256|HAMAP-Rule:MF_01917};
GN OrderedLocusNames=PA2155 {ECO:0000313|EMBL:AAG05543.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964 {ECO:0000313|EMBL:AAG05543.1, ECO:0000313|Proteomes:UP000002438};
RN [1] {ECO:0000313|EMBL:AAG05543.1, ECO:0000313|Proteomes:UP000002438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC 1C / PRS 101 / PAO1 {ECO:0000313|Proteomes:UP000002438};
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.Q., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R., Smith K.,
RA Spencer D., Wong G.K., Wu Z., Paulsen I.T., Reizer J., Saier M.H.,
RA Hancock R.E., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Catalyzes the phosphatidyl group transfer from one
CC phosphatidylglycerol molecule to another to form cardiolipin (CL)
CC (diphosphatidylglycerol) and glycerol. {ECO:0000256|HAMAP-
CC Rule:MF_01917}.
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_01917};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01917};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01917}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC subfamily. ClsB sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_01917}.
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DR EMBL; AE004091; AAG05543.1; -; Genomic_DNA.
DR PIR; B83377; B83377.
DR RefSeq; NP_250845.1; NC_002516.2.
DR RefSeq; WP_003113648.1; NZ_QZGE01000014.1.
DR AlphaFoldDB; Q9I1W0; -.
DR SMR; Q9I1W0; -.
DR STRING; 208964.PA2155; -.
DR PaxDb; 208964-PA2155; -.
DR GeneID; 881323; -.
DR KEGG; pae:PA2155; -.
DR PATRIC; fig|208964.12.peg.2254; -.
DR PseudoCAP; PA2155; -.
DR HOGENOM; CLU_038053_0_0_6; -.
DR InParanoid; Q9I1W0; -.
DR OMA; GEEYFPR; -.
DR OrthoDB; 9762009at2; -.
DR PhylomeDB; Q9I1W0; -.
DR BioCyc; PAER208964:G1FZ6-2195-MONOMER; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008808; F:cardiolipin synthase activity; IBA:GO_Central.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IBA:GO_Central.
DR CDD; cd09110; PLDc_CLS_1; 1.
DR CDD; cd09159; PLDc_ybhO_like_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 3.
DR HAMAP; MF_01917; Cardiolipin_synth_ClsB; 1.
DR InterPro; IPR030872; Cardiolipin_synth_ClsB.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR PANTHER; PTHR21248; CARDIOLIPIN SYNTHASE; 1.
DR PANTHER; PTHR21248:SF23; CARDIOLIPIN SYNTHASE B; 1.
DR Pfam; PF13091; PLDc_2; 2.
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|HAMAP-Rule:MF_01917};
KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01917};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01917};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01917};
KW Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01917};
KW Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_01917};
KW Reference proteome {ECO:0000313|Proteomes:UP000002438};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01917}.
FT DOMAIN 108..135
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 278..305
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 113
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 115
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 120
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 283
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 285
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 290
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
SQ SEQUENCE 401 AA; 46545 MW; F6CD96B0EA32D2D6 CRC64;
MNFPWRDGNR VELLINGEEY FPRLFQCIAE ARREILLETF IIFEDEVGRQ LQEALSAAAE
RGVEVQVTVD GYGTASLSPD YLARLTASGV RVHLFDPRPR LLGMRTNLFR RLHRKLVVID
RRQAFVGGIN YGEDHLVRRG NMAKQDYAVR VEGPVVRDIR QACLALLEPD ADYPPLRPSG
AGQPARVRLV IRDNDQSSDD IEREYLQAIR QARRRLLIAN AYFFPGYRLL RELRDAARRG
VRVDLVLQGM PDMPLVRLCS RLLYDYLLRE GVRIHEYCQR PLHGKVAVID DDWSTIGSSN
LDPLSLSLNL EANLVIRDVA FNGQLYQHLR ELARRHCRRI SRRHARRGYW WRAPLIFLGF
HFSRHFPAIA GWVPAHLPRL KSLEPRPSRR WQERQGQRGN P
//