ID A0A0K1FDB8_9MICO Unreviewed; 702 AA.
AC A0A0K1FDB8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=phospholipase C {ECO:0000256|ARBA:ARBA00012018};
DE EC=3.1.4.3 {ECO:0000256|ARBA:ARBA00012018};
GN ORFNames=ADJ73_08530 {ECO:0000313|EMBL:AKT52679.1};
OS Arsenicicoccus sp. oral taxon 190.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Arsenicicoccus.
OX NCBI_TaxID=1658671 {ECO:0000313|EMBL:AKT52679.1, ECO:0000313|Proteomes:UP000065578};
RN [1] {ECO:0000313|Proteomes:UP000065578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0371 {ECO:0000313|Proteomes:UP000065578};
RA Holder M.E., Ajami N.J., Petrosino J.F.;
RL Submitted (JUL-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}.
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DR EMBL; CP012070; AKT52679.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K1FDB8; -.
DR STRING; 1658671.ADJ73_08530; -.
DR KEGG; ars:ADJ73_08530; -.
DR PATRIC; fig|1658671.3.peg.1744; -.
DR Proteomes; UP000065578; Chromosome.
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; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 496..578
FT /note="Bacterial phospholipase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05506"
FT REGION 469..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 702 AA; 77324 MW; B8BA90B18BD4B3BF CRC64;
MDRRRFLQVA GATTAMTVLS DSIARAASIP ASRRHGSIRD VEHVVVLMQE NRSFDHYLGA
LRGVRGFGDP HPAVLPSGKD VWHQSDGTRE VLPFRPDQDQ LGHAFLEGLP HGWWDGQMAV
NRGRYDRWLP AKGTTTMAHL ERRDAAFHYQ LADAFTVCDG YYCSFIGNTD PNRYYLWSGW
VGNDGKGGGP ELYNEELGYG WTTYPERLEA AGVSWKVYQD EGTGLDAAGS WGWTQDPYIG
NYGDTSLLYF NSYRNAKPGD PLYEKARRGT TARTGDDYFR ILREDVRTGR LPAVSYISAP
EAFSEHSNWP TAYGAWYIAQ VLDALTSNPE VWSRTALFIT YDENDGFFDH LVPPMATNPD
IPGASTVSTE YEYFPGKAGD KRFPSGAYGA GPRVPMWVVS PWSTGGWVCS EAFDHTSVIR
FMEKRFGVRE PQITPWRRAV FGDLTSAFDF SRTPATPPRL MDVAGWAPTD RQRHPDYKPV
PPAAGTMPRQ EPGTRPARPL GYDLRLDERP SDQGLTLTLT NRGRLGAALQ ARLLEPADAP
RSYTVEAGRS VSATLPATGA YHVDVHGPNG FFRSYAGDRS QDAVTVSLEP QGRSGRLRLV
VTRLGREVDV EITSAYPAAL RAGGDAEVSD EQGGDEQGGG SASLRDHGRG KGRSRSAVRV
DTRRSGGWYD LTVTVPGTGF RRVLAGHLET GAPSVSDPQL GR
//
