ID A0A1G5KN09_9ACTN Unreviewed; 732 AA.
AC A0A1G5KN09;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=phospholipase C {ECO:0000256|ARBA:ARBA00012018};
DE EC=3.1.4.3 {ECO:0000256|ARBA:ARBA00012018};
GN ORFNames=SAMN02745898_106380 {ECO:0000313|EMBL:SCZ01470.1};
OS Streptomyces sp. 136MFCol5.1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1172182 {ECO:0000313|EMBL:SCZ01470.1, ECO:0000313|Proteomes:UP000199326};
RN [1] {ECO:0000313|EMBL:SCZ01470.1, ECO:0000313|Proteomes:UP000199326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=136MFCol5.1 {ECO:0000313|EMBL:SCZ01470.1,
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; FMVI01000006; SCZ01470.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5KN09; -.
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; 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:UP000199326};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 529..616
FT /note="Bacterial phospholipase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05506"
FT DOMAIN 624..705
FT /note="Bacterial phospholipase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05506"
FT REGION 489..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 732 AA; 80849 MW; 85AC8AC880722D14 CRC64;
MPSPTSRRDF LRRSATTLGA ATAASVLPGS ISRALAVDAA VRTGTVKDVE HVVILMQENR
GFNHYFGTMR GVRGFGDRFP IPLESGKPVW YQSDGAREIP PYHLDPERSS ALLIPSTPHS
FADAQAAWNQ GKLGQWPKYK TEYSMGYYRR DDIPFQFALA EAFTICDSYH CSITTGTDPN
RITFWSGSNF NPELGRQGVN SGPDQSEPNN LRCWITGKWV PDAWPQTYKY ASNAFAWDTI
PDVLERAGIS WHIYQDMNDN WTGAMNGCLA FGSFRNAQPG TPVYEHGMTG GPDFLDRLRQ
DVLDGTLPQV SWVLTTASNS EHPGAGSSPT HGGNFTADVL DALTANPEVW SKTVFLLTFD
ENDGLFDHVP APAVPSYNLD GTLAGKSTVP VDGEYFDASG KPSSWLKADD TVTGTTRPWG
MGPRVPLYVV SPWSRGGWVD SEVFDHTSVG MFLEQRFGVQ IDAISPWHRA VSGDLTSAFD
FKHPNRQRFP ELPDQSDWAT SDAHQRTLPS PKAPTAPEPL FQERGTRYSR ALPYELHTDA
STDHGAGTVT LRFLNSGHKG AVFHVYDRLH LDRIPRRYTV EAGKRLADVW DASATDSGAY
DLEVHGPGGF FRSFTGSTAS KADPELRVRY DRHGKSVVLT VHNPGPKAVT LHVEPHAYRF
TEPRTIHVPS HKEVERRWSL NPSGHWYDFT VTVDGSSLER RFAGRVETGK DGISDPAMAA
HIQQAEGVVA AN
//
