ID A0A1E5PYK0_9ACTN Unreviewed; 688 AA.
AC A0A1E5PYK0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=phospholipase C {ECO:0000256|ARBA:ARBA00012018};
DE EC=3.1.4.3 {ECO:0000256|ARBA:ARBA00012018};
GN ORFNames=BGK67_27405 {ECO:0000313|EMBL:OEJ34566.1};
OS Streptomyces subrutilus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=36818 {ECO:0000313|EMBL:OEJ34566.1, ECO:0000313|Proteomes:UP000095705};
RN [1] {ECO:0000313|EMBL:OEJ34566.1, ECO:0000313|Proteomes:UP000095705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10-1-1 {ECO:0000313|EMBL:OEJ34566.1,
RC ECO:0000313|Proteomes:UP000095705};
RA Chen X.;
RT "The complete genome of Streptomyces subrutilus 10-1-1.";
RL Submitted (AUG-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}.
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:OEJ34566.1}.
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DR EMBL; MEHK01000001; OEJ34566.1; -; Genomic_DNA.
DR RefSeq; WP_069922757.1; NZ_MEHK01000001.1.
DR AlphaFoldDB; A0A1E5PYK0; -.
DR STRING; 36818.BGK67_27405; -.
DR OrthoDB; 4181857at2; -.
DR Proteomes; UP000095705; 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:UP000095705};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 496..581
FT /note="Bacterial phospholipase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05506"
FT DOMAIN 589..669
FT /note="Bacterial phospholipase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05506"
FT REGION 465..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 688 AA; 74525 MW; 67197EF94392446D CRC64;
MAELNRRRFL QLAGGATALT MLNESIARAA AIPAQGTTGT IADVEHIVVL MQENRSFDHY
YGALRGVRGF GDPRPVTLPS GKSVWHQSDG TKETLPFRPP SDDLGMEFLQ GLNHDWAGGQ
SAFNKGRYDN WVPAKTPTTM AYLTRDDIPF HYALADAFTI CDAYHCSFIG STDPNRYYLW
SGHTGNDGRG GGPVLDNAEL GYGWTTYPER LEAAGISWKV YQDIGDGLDA AGHWGWINDA
YRGNYGDNSL LYFNSYRNAQ PGDPLFDKAR TGTNAKAGEG YFDRLRADVA AGTLPQVSWI
AAPEAFSEHS NWPSNYGAWY IAQVLDALTS NPDVWARTAL FITYDENDGF FDHVVPPYAP
ADADQGLSTT PTALDVFPGK AGYVAGPYGL GPRVPMLVVS PWSTGGYSCS ETFDHTSVIR
FMEQRFGVRE PNISPWRRAV CGDLTSAFDF GRSDTGAVEL PDTAAWEPQD RDRHPDFRAP
APAVGSMPRQ EKGMRPTRAL KYAPYVDGTA LTAEGRFRLA FSGGPDLGAQ FYVTSGNRTD
APWTYTTEAG KSIADTWNTR YSGGVTDLTV HGPNGFLRGF RNPGTTPGPE VTARHNATTG
NLDLTLTNAG GSTAALTVTN SYGGGPKRLT VAKGATVTYS VSLKNTRRWY DVTVTASGAP
DFLRRFAGKV ETGAAGLSDP AILTDQSS
//
