ID A0A1B1AXS9_9ACTN Unreviewed; 609 AA.
AC A0A1B1AXS9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=phospholipase C {ECO:0000256|ARBA:ARBA00012018};
DE EC=3.1.4.3 {ECO:0000256|ARBA:ARBA00012018};
GN ORFNames=AVL59_18440 {ECO:0000313|EMBL:ANP51337.1};
OS Streptomyces griseochromogenes.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68214 {ECO:0000313|EMBL:ANP51337.1, ECO:0000313|Proteomes:UP000092659};
RN [1] {ECO:0000313|EMBL:ANP51337.1, ECO:0000313|Proteomes:UP000092659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14511 {ECO:0000313|EMBL:ANP51337.1,
RC ECO:0000313|Proteomes:UP000092659};
RA Wu L.;
RT "Complete genome sequence of Streptomyces griseochromogenes ATCC 14511, the
RT Blasticidin S producer.";
RL Submitted (JUN-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; CP016279; ANP51337.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B1AXS9; -.
DR STRING; 68214.AVL59_18440; -.
DR KEGG; sgs:AVL59_18440; -.
DR OrthoDB; 4181857at2; -.
DR Proteomes; UP000092659; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0034480; F:phosphatidylcholine phospholipase C activity; IEA:UniProtKB-EC.
DR CDD; cd16013; AcpA; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 2.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR007312; Phosphoesterase.
DR InterPro; IPR006311; TAT_signal.
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 PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Secreted {ECO:0000256|ARBA:ARBA00022512}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..609
FT /note="phospholipase C"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039382918"
FT TRANSMEM 581..603
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 215..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 609 AA; 63992 MW; B2BAED6A7A809A8E CRC64;
MASRGRRAAM RSLGALAGAA ALTVLGSNAP GWAAAPAGAP GGHSSTTTPI KHVVVLFDEN
ISFDHYFATY PKAANSDGTK FKASKNTPKD IDTLAHAGLL KHNPNQYAPK RLSPAQAMTC
DQNHSYGPEQ YAYNGGKADQ FVQNTEVDKC SGGLFGEPGL AMDYYDGNTV TALWNYAQHY
SLGDRSYSSN YGPSTPGALN LISGNTHGVI SVDPATGKKT ATPDPYAVKS PDAKGVGTVI
NDPDPAFDDC SGKDHTSTNA LAALQGRNIG DLLNAKKVSW GWFQGGFRPS AAWNGTSGSY
AKCDITHTNV GGAAVADYSP HHNPFSYYES TANPHHLPPK SVSEIGHNGQ ANHNYDLTDF
TAAAKAGKLP AVSFVKAGEY QDGHAGYSDP LDEQHFLVKQ INAIQSSPQW KSTAIVVAYD
DSDGWYDHAY AAPRNGSKDT SVGSNGKATD SPACQNGPKA AGGYADRCGP GTRQPLLVIS
PYSKVNKVDH TQTDQASLTR FIEDNWHTGR IGDHSFDASA GSLAGMFDFR HPNNKQVLLN
SDGSVKSVGP IKHVAAVATS ITPGPAMQNT AASTGTSGLP VLPLSLGVGA LLAAGVTGTY
LTMRRRQHA
//
