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Database: UniProt
Entry: A0A0J6XDP8_9ACTN
LinkDB: A0A0J6XDP8_9ACTN
Original site: A0A0J6XDP8_9ACTN 
ID   A0A0J6XDP8_9ACTN        Unreviewed;       690 AA.
AC   A0A0J6XDP8;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=phospholipase C {ECO:0000256|ARBA:ARBA00012018};
DE            EC=3.1.4.3 {ECO:0000256|ARBA:ARBA00012018};
GN   ORFNames=ACS04_31480 {ECO:0000313|EMBL:KMO94030.1};
OS   Streptomyces roseus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=66430 {ECO:0000313|EMBL:KMO94030.1, ECO:0000313|Proteomes:UP000035932};
RN   [1] {ECO:0000313|EMBL:KMO94030.1, ECO:0000313|Proteomes:UP000035932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31245 {ECO:0000313|EMBL:KMO94030.1,
RC   ECO:0000313|Proteomes:UP000035932};
RA   Cruz-Morales P., Martinez-Guerrero C., Morales-Escalante M.A.,
RA   Yanez-Guerra L.A., Kopp J.F., Feldmann J., Ramos-Aboites H.E.,
RA   Barona-Gomez F.;
RT   "Recapitulation of the evolution of biosynthetic gene clusters reveals
RT   hidden chemical diversity on bacterial genomes.";
RL   Submitted (JUN-2015) 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-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:10604,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:295975; EC=3.1.4.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00023550};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10605;
CC         Evidence={ECO:0000256|ARBA:ARBA00023550};
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000256|ARBA:ARBA00004191}.
CC   -!- SIMILARITY: Belongs to the bacterial phospholipase C family.
CC       {ECO:0000256|ARBA:ARBA00009717}.
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:KMO94030.1}.
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DR   EMBL; LFML01000150; KMO94030.1; -; Genomic_DNA.
DR   RefSeq; WP_048480233.1; NZ_LFML01000150.1.
DR   AlphaFoldDB; A0A0J6XDP8; -.
DR   STRING; 66430.ACS04_31480; -.
DR   PATRIC; fig|66430.4.peg.2628; -.
DR   OrthoDB; 4181857at2; -.
DR   Proteomes; UP000035932; Unassembled WGS sequence.
DR   GO; GO:0034480; F:phosphatidylcholine phospholipase C activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR   CDD; cd16014; PLC; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 2.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR017767; Bact_PC-PLC.
DR   InterPro; IPR007312; Phosphoesterase.
DR   InterPro; IPR008475; PLipase_C_C.
DR   InterPro; IPR006311; TAT_signal.
DR   NCBIfam; TIGR03396; PC_PLC; 1.
DR   PANTHER; PTHR31956:SF8; ACID PHOSPHATASE PHOA (AFU_ORTHOLOGUE AFUA_1G03570); 1.
DR   PANTHER; PTHR31956; NON-SPECIFIC PHOSPHOLIPASE C4-RELATED; 1.
DR   Pfam; PF04185; Phosphoesterase; 1.
DR   Pfam; PF05506; PLipase_C_C; 2.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035932};
KW   Secreted {ECO:0000256|ARBA:ARBA00022512};
KW   Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT   DOMAIN          499..582
FT                   /note="Bacterial phospholipase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05506"
FT   DOMAIN          590..670
FT                   /note="Bacterial phospholipase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05506"
FT   REGION          460..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   690 AA;  74598 MW;  02E8FB93B0C5EA39 CRC64;
     MAELNRRRFL QLTGGAAALT LLNESIARAA AIPAQGTTGT IADVEHVVVL MQENRSFDHY
     FGALRGIRGF GDPRPVTLPS GKSVWHQTDN AGKETLPFRP PSDDLGMEYL QGLNHDWAGG
     QSAFNKGKYD NWVPAKTPAT MAHLTREDIP FHYALADAFT ICDAYHCSFI GSTDPNRYYL
     WSGHTGNDGK GGGPVLNNAE AGYGWTTYPE RLEQAGISWK VYQDIGNGLD AAGSWGWIND
     AFRGNYGDNS LLYFNNYRTA QPGDPLYEKA RTGTDARTGE GYFDRLRADV AAGTLPQVSW
     IAAPEAFSEH SNWPANFGAW YIAQVLDALT SNPDVWARTA LFITYDENDG FFDHVVPPYA
     PANANQGLST VSTTLDVFPG AAGYVAGPYG LGPRVPMLVV SPWSTGGYSC SETFDHTSVI
     RFMEKRFGVR EPNISPWRRA VCGDLTSAFD FARKDTGTVR LPDTGPWEPQ DRERHPNFLA
     TPPAVGTMPR QEKGLCNTRP LKYAPYVDGA ALTGEGKFRL TFSGGPDLGA QFYVTSGNRT
     DAPWTYTTEA GKSVSDTWNT AYSTGATDLT VHGPNGFLRG FRNPGTAPGP EVTARHNAAT
     GNLDLTLTNA GASTATLTVT NAYGGGPKRL TVAKGATLTY SVPLRSTRRW YDVTVTASEF
     PDFGRRFAGK VETGAAGLSD PGILTEQGGS
//
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