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Database: UniProt
Entry: A0A117R2N8_9ACTN
LinkDB: A0A117R2N8_9ACTN
Original site: A0A117R2N8_9ACTN 
ID   A0A117R2N8_9ACTN        Unreviewed;       684 AA.
AC   A0A117R2N8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=phospholipase C {ECO:0000256|ARBA:ARBA00012018};
DE            EC=3.1.4.3 {ECO:0000256|ARBA:ARBA00012018};
GN   ORFNames=AQJ54_14540 {ECO:0000313|EMBL:KUN67754.1};
OS   Streptomyces griseorubiginosus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=67304 {ECO:0000313|EMBL:KUN67754.1, ECO:0000313|Proteomes:UP000054375};
RN   [1] {ECO:0000313|EMBL:KUN67754.1, ECO:0000313|Proteomes:UP000054375}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40469 {ECO:0000313|EMBL:KUN67754.1,
RC   ECO:0000313|Proteomes:UP000054375};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces griseorubiginosus DSM 40469, type
RT   strain for the species Streptomyces griseorubiginosus.";
RL   Submitted (OCT-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:KUN67754.1}.
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DR   EMBL; LMWV01000008; KUN67754.1; -; Genomic_DNA.
DR   RefSeq; WP_062237624.1; NZ_KQ948736.1.
DR   AlphaFoldDB; A0A117R2N8; -.
DR   Proteomes; UP000054375; 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   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054375};
KW   Secreted {ECO:0000256|ARBA:ARBA00022512};
KW   Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT   DOMAIN          497..583
FT                   /note="Bacterial phospholipase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05506"
FT   DOMAIN          599..668
FT                   /note="Bacterial phospholipase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05506"
FT   REGION          460..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..478
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   684 AA;  75000 MW;  D8D5EAE6A589B2BF CRC64;
     MADVNRRRFL QLAGATTAFS ALSNSIQRAA ALPAHHRTGT IEDVEHVVVL MQENRSFDHY
     FGSLRGVRGF GDPRPVTLDS SKSVWHQTDR NGKEILPFRP EANDLGMQFI QDLPHGWNDG
     HAAFNGGKYD KWVPNKGSTT MAYLTREDIP FHYALADSFT ICDAYHCSFI GSTDPNRYYM
     WTGYTGNDGQ GGGPVLGNDE AGYGWTTYPE RLEKAGVSWK IYQDVGDGLD ANGSWGWIPD
     AYRGNYGDNS LLYFNQYRNA KPGDPLYDKA RTGTDYTKGE GYFDQLKADV KAGKLPQVSW
     IVAPEAFTEH PNWPANYGAW YVAQVLDALT SDPKVWAKTA VFITYDENDG FFDHVVPAYP
     AGSAAQGKST VDPALDLFQG SASHPAGPYG LGQRVPMLVV SPWSKGGYVC SETLDHTSII
     RFLERRFGVH EPNISPWRRA VCGDLTAAFD FSRKDTKPVA LPDTDGFEPP DRERHPDYVP
     VPPAVGALPR QERGLRPARP LKYAPHVDGS VDAKGGRFTL AFASGAKAGA AFLVTSGNRT
     DGPWSYTTEA GKSVSDTWNS AYSKGSYDLT VHGPNGFLRS FKGSNKTAGP EVTARHSGDD
     IELTFTNSGS GLVRLKVESG YGDRVRTFTV RPGTTVRHTF GLARSRRWYD LTVTADADPA
     FLRRFAGHVE NGRPGVSDPA VITG
//
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