ID A0A0B4S2V2_9FIRM Unreviewed; 514 AA.
AC A0A0B4S2V2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Phospholipase {ECO:0000313|EMBL:AIZ36971.1};
GN ORFNames=NW74_06295 {ECO:0000313|EMBL:AIZ36971.1};
OS Parvimonas micra.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Parvimonas.
OX NCBI_TaxID=33033 {ECO:0000313|EMBL:AIZ36971.1, ECO:0000313|Proteomes:UP000031386};
RN [1] {ECO:0000313|EMBL:AIZ36971.1, ECO:0000313|Proteomes:UP000031386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCOM 1535 / ChDC B708 {ECO:0000313|Proteomes:UP000031386};
RA Kook J.-K., Park S.-N., Lim Y.K., Roh H.;
RT "Complete genome sequence of Parvimonas micra KCOM 1535 (= ChDC B708).";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP009761; AIZ36971.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B4S2V2; -.
DR STRING; 33033.NW74_06295; -.
DR KEGG; pmic:NW74_06295; -.
DR Proteomes; UP000031386; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0008808; F:cardiolipin synthase activity; IEA:InterPro.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:InterPro.
DR CDD; cd09154; PLDc_SMU_988_like_1; 1.
DR CDD; cd09160; PLDc_SMU_988_like_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
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 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Reference proteome {ECO:0000313|Proteomes:UP000031386};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 38..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 245..272
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 427..454
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 514 AA; 59853 MW; 6B5B05C920E8A593 CRC64;
MKNFFNFIFS RIFFIICMVL IQLMFLTVFL IYFNRYFIYL YGINLIVGLI FTFIIINDNI
NPAFKITWIL IVVVLPFLGG IIYLTFGEKR LLKSVKKRLF NFSIKFKDSM DLSKDYDIEN
LNDSDMNVYR QAKYINCATG SPVFFNTETK YFASGEDSFE EYLNDLKTAE KFIFMEYFII
SEGFFLDSVL NILKQKVKNG VDVKIIIDDI GSILTLSNKT LEEIRNLGIK VVEFNQVKGI
VLPKHNNRTH RKMTIIDGKI AYTGGINIAD EYINLYEKYG YWKDSVLKLE GHAVASFINM
FISLWDYSTG ENTDILSLYD KSDLEKKSNI RDDLGVVIPF SETPVMESTS ENMYLNMIRR
ANRYIYITTP YLIITWEMEK ALISAAKTGV DVRIITPHIP DKKYVHLLTR SFYKNLVENG
VKIYEFKKGF IHAKNFLCDD GFVVIGSINL DYRSLYLHFE CAVWTFGTPI VSDVKEDFEN
TLKDSMEITP EWIKSRKLIT RILQSLLKLF APLM
//
