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Database: UniProt
Entry: A8PK22_9COXI
LinkDB: A8PK22_9COXI
Original site: A8PK22_9COXI 
ID   A8PK22_9COXI            Unreviewed;       178 AA.
AC   A8PK22;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE            EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN   ORFNames=RICGR_0232 {ECO:0000313|EMBL:EDP46030.1};
OS   Rickettsiella grylli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Rickettsiella.
OX   NCBI_TaxID=59196 {ECO:0000313|EMBL:EDP46030.1, ECO:0000313|Proteomes:UP000054075};
RN   [1] {ECO:0000313|EMBL:EDP46030.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Seshadri R., Federici B.A.;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDP46030.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Myers G.S.;
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC         sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445,
CC         ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000798};
CC   -!- SIMILARITY: Belongs to the phospholipase D family.
CC       {ECO:0000256|ARBA:ARBA00008664}.
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:EDP46030.1}.
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DR   EMBL; AAQJ02000001; EDP46030.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8PK22; -.
DR   STRING; 59196.RICGR_0232; -.
DR   eggNOG; COG1502; Bacteria.
DR   OrthoDB; 5294698at2; -.
DR   Proteomes; UP000054075; Unassembled WGS sequence.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006793; P:phosphorus metabolic process; IEA:UniProt.
DR   CDD; cd09170; PLDc_Nuc; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 1.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   PANTHER; PTHR43856; CARDIOLIPIN HYDROLASE; 1.
DR   PANTHER; PTHR43856:SF1; MITOCHONDRIAL CARDIOLIPIN HYDROLASE; 1.
DR   Pfam; PF13091; PLDc_2; 1.
DR   SMART; SM00155; PLDc; 1.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 1.
DR   PROSITE; PS50035; PLD; 1.
PE   3: Inferred from homology;
KW   Endonuclease {ECO:0000313|EMBL:EDP46030.1};
KW   Hydrolase {ECO:0000313|EMBL:EDP46030.1};
KW   Nuclease {ECO:0000313|EMBL:EDP46030.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..178
FT                   /note="phospholipase D"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002727758"
FT   DOMAIN          113..140
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   178 AA;  20117 MW;  6C4855C639547B4D CRC64;
     MLKKLFLVFL LSPCLITTSF AINKIKNCPT LQACFTPGQN CTEEITDVID AAKKSIFVQA
     YSFTSAAIAE HLVAAKKRGV NVNVILDKSQ RTQRYSASHF LIHQHIPCWI DYKPAIAHNK
     VMIIDEKEVI TGSFNFTKAA QAHNAENLLV IRDHSLAQLY LKNWQRRQAV SRSLNPHI
//
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