ID A0A1G5G3R7_9ACTN Unreviewed; 702 AA.
AC A0A1G5G3R7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=phospholipase C {ECO:0000256|ARBA:ARBA00012018};
DE EC=3.1.4.3 {ECO:0000256|ARBA:ARBA00012018};
GN ORFNames=SAMN02745898_10259 {ECO:0000313|EMBL:SCY45977.1};
OS Streptomyces sp. 136MFCol5.1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1172182 {ECO:0000313|EMBL:SCY45977.1, ECO:0000313|Proteomes:UP000199326};
RN [1] {ECO:0000313|EMBL:SCY45977.1, ECO:0000313|Proteomes:UP000199326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=136MFCol5.1 {ECO:0000313|EMBL:SCY45977.1,
RC ECO:0000313|Proteomes:UP000199326};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FMVI01000002; SCY45977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5G3R7; -.
DR OrthoDB; 4181857at2; -.
DR Proteomes; UP000199326; 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 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; 2.
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:UP000199326};
KW Secreted {ECO:0000256|ARBA:ARBA00022512}; Signal {ECO:0000256|SAM:SignalP};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..702
FT /note="phospholipase C"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039627269"
FT DOMAIN 518..599
FT /note="Bacterial phospholipase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05506"
FT DOMAIN 605..692
FT /note="Bacterial phospholipase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05506"
SQ SEQUENCE 702 AA; 77015 MW; B7EB227DA01B0435 CRC64;
MTTDISRRRL LALGGGALGA AAAGSLLPPS LQAALAAQPV RPAGSGGLGD IRHVVILMQE
NRSFDHYFGT LRGVRGFGDR NAIELPSGKP VFEQPGASDT SVLPFPIRDA AATQKKDLQY
VNALDHSWSG GGKAWAGGWM NGWVTAKTAA TMAYYDRRDI PLHYELADTF TVCDAYHSSI
HTSTSPNRNH LWSGKTGFEA NGRRAVGNDA YSEGTHPGYG WSTYAERLEK AGHSWKTYTE
WENFTDNQIE FFATFKAIAR KALAKTGGHT YMESFYAAVR DTDDAAERER LLGLLEDGVA
TLTEAERSLF ERGLRRVETG TLADAFAEDV AAGTLPEVSY LVPSAVDSEH PSVSSPIHSA
TIVYKVLDAL GRHPDVWRHT AVIINYDEND GFFDHVPPPV APPEVTDEQW ESKPTGLGVR
VPLLVVSPWT VGGFVCSEVF DHTSVIRFLE RWTGVREPNI SDWRRTVTGD LTSAFDFTRG
RRRPEMEQPG VIPPFSGRWV PKPPAVQQMP VQEPGARPAR PLPYQPDAQA KIVDGAVRVA
LSNTGRSSAH FALYPYAGEF PVPQHRDVRG TAIWTVPVSG EAYRFTVTGP NGFRREFAGT
AEGGPEVATW VDAHERDVHL TLRNTGRRTL TYTVRPLGYV DEADLRDWTR TIKVKPGRSR
TVVHSAADAH GWYDLAVTVD GDDAFSRRLM GHIENGRASV SG
//
