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Database: UniProt
Entry: A0A117RRT5_9ACTN
LinkDB: A0A117RRT5_9ACTN
Original site: A0A117RRT5_9ACTN 
ID   A0A117RRT5_9ACTN        Unreviewed;       683 AA.
AC   A0A117RRT5;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=phospholipase C {ECO:0000256|ARBA:ARBA00012018};
DE            EC=3.1.4.3 {ECO:0000256|ARBA:ARBA00012018};
GN   ORFNames=AQJ67_02765 {ECO:0000313|EMBL:KUO05766.1};
OS   Streptomyces caeruleatus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=661399 {ECO:0000313|EMBL:KUO05766.1, ECO:0000313|Proteomes:UP000053429};
RN   [1] {ECO:0000313|EMBL:KUO05766.1, ECO:0000313|Proteomes:UP000053429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-24802 {ECO:0000313|EMBL:KUO05766.1,
RC   ECO:0000313|Proteomes:UP000053429};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces caeruleatus NRRL B-24802, type
RT   strain for the species Streptomyces caeruleatus.";
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:KUO05766.1}.
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DR   EMBL; LMWY01000003; KUO05766.1; -; Genomic_DNA.
DR   RefSeq; WP_062716330.1; NZ_KQ948924.1.
DR   AlphaFoldDB; A0A117RRT5; -.
DR   STRING; 661399.AQJ67_02765; -.
DR   OrthoDB; 4181857at2; -.
DR   Proteomes; UP000053429; 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:UP000053429};
KW   Secreted {ECO:0000256|ARBA:ARBA00022512};
KW   Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT   DOMAIN          496..582
FT                   /note="Bacterial phospholipase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05506"
FT   DOMAIN          598..667
FT                   /note="Bacterial phospholipase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05506"
FT   REGION          452..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..480
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   683 AA;  75054 MW;  6476C10E9457F74E CRC64;
     MPEVNRRRFL QLAGTTTAFT ALSSSIQRAA AIPANHRTGS IEDVEHIVVL MQENRSFDHY
     FGKLRGVRGF GDPRPVKRDD GKSIWHQSNG GKDILPFHPD AGDLGMQFLE GLPHGWTDGQ
     QAYNGGKYDK WVPAKGTTTM AYLTREDIPF HYALADAFTV CDAYHCSFIG STDPNRYYMW
     TGCTGNDGTG GGPVLGNDEL GYGWTTYPER LEQAGVSWKI YQDIGDGLDA KGSWGWIQDA
     YRGNYGDNSL LYFNKYRDAK PGDPWYDKAR TGTDAKSGEG YFDRLKADVK AGKLPQISWI
     AAPEAFSEHS NWPSNYGAWY IAQVLDALTS NPEVWSKTAL FITYDENDGF FDHVVPPLPP
     KDASRGKSTV DVSLDLYKGD SNRPAGPYGL GPRVPMLVVS PWSKGGYVCS ETLDHTSILR
     FMERRFGVRE TNISPWRRAV CGDLTSAFDF SRKDSRPAAL PGTDEYEPQD RERHPDYKPT
     PPADPDMPRQ ERGLRPTRPL RYAPHVDGSV DAAAGKFTLA FASGAKAGAA FHVTSGNRTD
     GPWTYTTEAG KSIADTWNSA YSNGSYDLTV HGPGGFVRWF KGSNKTAGPE VTARHTGDDV
     ELTLTNRGTA SVRLKIANGY GGRATTVTVR PGATVCRTVD LAGSRRWYDL TVAADADPAF
     LRRFAGHVEN GRPGVSDPAI ITE
//
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