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Database: UniProt
Entry: B2XRL4_CHLTH
LinkDB: B2XRL4_CHLTH
Original site: B2XRL4_CHLTH 
ID   B2XRL4_CHLTH            Unreviewed;       275 AA.
AC   B2XRL4;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE            EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
OS   Chlamydia trachomatis.
OC   Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=813 {ECO:0000313|EMBL:ABX82350.1};
RN   [1] {ECO:0000313|EMBL:ABX82350.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C/TW-3 {ECO:0000313|EMBL:ABX82350.1};
RX   PubMed=18199030; DOI=10.1086/525285;
RA   Kari L., Whitmire W.M., Carlson J.H., Crane D.D., Reveneau N., Nelson D.E.,
RA   Mabey D.C., Bailey R.L., Holland M.J., McClarty G., Caldwell H.D.;
RT   "Pathogenic diversity among Chlamydia trachomatis ocular strains in
RT   nonhuman primates is affected by subtle genomic variations.";
RL   J. Infect. Dis. 197:449-456(2008).
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};
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DR   EMBL; EU121606; ABX82350.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2XRL4; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006793; P:phosphorus metabolic process; IEA:UniProt.
DR   CDD; cd09116; PLDc_Nuc_like; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
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; 2.
DR   SMART; SM00155; PLDc; 2.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS50035; PLD; 2.
PE   4: Predicted;
FT   DOMAIN          70..93
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          212..239
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   275 AA;  30958 MW;  CEA1080708DB4237 CRC64;
     MLCDAILQAN RIITMRIFNI GSPEIIRALI QAVRRNIPVV VSAWNFPNLS NWDRKSELCV
     ELRGNPQICL HKKTTLIDNQ LAIIGTANYT KSSFFKDINL TALIQNPALY SLILRGTRGS
     VSIGSQTISY YPLPFPQSNT KTLPIIQEIQ KAQRTIKIAM SIFSHPEIFL ALEQAHLRGV
     TITIVINKKE SAHTLDILHR ISALLLLKSV TTVDSLHAKI CLIDDQTLIF GSPNWTYHGM
     HKNLEDLLIV TPLTPKQIYS IQEIWAFLLK NSSPV
//
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