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Database: UniProt
Entry: A0A1I2J5S2_9ACTN
LinkDB: A0A1I2J5S2_9ACTN
Original site: A0A1I2J5S2_9ACTN 
ID   A0A1I2J5S2_9ACTN        Unreviewed;      1042 AA.
AC   A0A1I2J5S2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=phospholipase C {ECO:0000256|ARBA:ARBA00012018};
DE            EC=3.1.4.3 {ECO:0000256|ARBA:ARBA00012018};
GN   ORFNames=SAMN05216251_116124 {ECO:0000313|EMBL:SFF50045.1};
OS   Actinacidiphila alni.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Actinacidiphila.
OX   NCBI_TaxID=380248 {ECO:0000313|EMBL:SFF50045.1, ECO:0000313|Proteomes:UP000199323};
RN   [1] {ECO:0000313|EMBL:SFF50045.1, ECO:0000313|Proteomes:UP000199323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3510 {ECO:0000313|EMBL:SFF50045.1,
RC   ECO:0000313|Proteomes:UP000199323};
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; FONG01000016; SFF50045.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2J5S2; -.
DR   Proteomes; UP000199323; 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; 2.60.120.200; -; 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   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199323};
KW   Secreted {ECO:0000256|ARBA:ARBA00022512}; Signal {ECO:0000256|SAM:SignalP};
KW   Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..1042
FT                   /note="phospholipase C"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011595011"
FT   DOMAIN          529..609
FT                   /note="Bacterial phospholipase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05506"
FT   DOMAIN          616..694
FT                   /note="Bacterial phospholipase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05506"
FT   REGION          179..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1042 AA;  111276 MW;  A316CD82F677192E CRC64;
     MSPELSRRTL LGSAAGAALL SALPMSVRTA LAAPARPGSL EDIAHVVVLM QENRSFDHYY
     GTMQGVRGYG DRTAVRGVNG RPVWAQPDPS RAEGHLLPFA MNAAHTNAYQ QGAPAFGFTD
     SMNARNDGLA DGYVTRRGGG WLGQGYYEPA DMPFYNALAS VFTICDNYHA AMETSTNPNR
     EHFMTGTSGG TVRDTPVTDN TETSAGYEWT TYAERLEAAG ISWKTYQAQE NFDDNALAWF
     APFHRAKPGE PLYERGMRRA GDPAQAGDPW AMGDALVAAF AADVAADALP QVSWLVAPAA
     LSEHASYAPP DGEDLTARLL AALADHPAVF AKTAFILNYD EHGGFFDHVL PPVPPMGAGR
     GKSTVSTDGE IVVRVTKSGS TYHRVVGYDG RYRVKAADGS LTWSDTLPAG ESVVAGPFPL
     GLGIRVPMIV ASPWTRGGVV DSTVYDHTSV IKFLEKRFGV REPNISEWRR AVTGDLTSVF
     DFSGDEPKWP SLPDTSGNRR KVTDSGKLPA PTVPSPQVPP VQQRGSRAAR PSPYALRMRS
     HVRGASLELD FVNLGTQAAV FAAYPAPGSR PRFFTVGARD RLSDAWQIDA DGYDLRVNGP
     NGSLWHFRGG AARLEAQLTE DPVARHLEIE LRNDERGPRT FRIGDLAYRG GVHEMRVGGG
     ATRSITLGVD HDGWYDVAVT DADDPFFLRR FAGKVADHRP GVTDPAMGAP DALTAEVRLS
     AASPAIDEPV VLPGRPSTVT AVLTATVAVT KLEAAPVVPA GWEVRTVTAP PARLSAGASA
     TAVWQVTPPA ALPSDTTHRV LVTARGTAGN RLALADCEVA ARTAPSMDGY LLGEDFESLA
     GQLKPAVTLP VPADVLGWTA TAPACWSVVN AAGMPQGSVE EQGWTFMTKR FWTASDSQDR
     GNFSRALGII AVADPDDWDD HGSPSGKGTF DSTLVSPAVP VPAGATVLHL GFDSHYRQEA
     PQTATVSAVF DTGEETVLLT YSGAATGNDN AGHDAENQLV TRTVDVPSGA RTVTLKFRMF
     NAGNNWYWAI DHIRLGTRPV TD
//
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