ID M2YY05_9PSEU Unreviewed; 703 AA.
AC M2YY05;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, 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=H074_16616 {ECO:0000313|EMBL:EME59807.1};
OS Amycolatopsis decaplanina DSM 44594.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1284240 {ECO:0000313|EMBL:EME59807.1, ECO:0000313|Proteomes:UP000054226};
RN [1] {ECO:0000313|EMBL:EME59807.1, ECO:0000313|Proteomes:UP000054226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44594 {ECO:0000313|EMBL:EME59807.1,
RC ECO:0000313|Proteomes:UP000054226};
RX PubMed=23558534;
RA Kaur N., Kumar S., Bala M., Raghava G.P., Mayilraj S.;
RT "Draft Genome Sequence of Amycolatopsis decaplanina Strain DSM 44594T.";
RL Genome Announc. 1:E0013813-E0013813(2013).
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:EME59807.1}.
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DR EMBL; AOHO01000049; EME59807.1; -; Genomic_DNA.
DR AlphaFoldDB; M2YY05; -.
DR PATRIC; fig|1284240.4.peg.3375; -.
DR Proteomes; UP000054226; 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 Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 526..609
FT /note="Bacterial phospholipase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05506"
FT DOMAIN 628..690
FT /note="Bacterial phospholipase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05506"
FT REGION 487..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 703 AA; 77340 MW; A03367123E3F3118 CRC64;
MTFMFLGQGS GMPELSRRTL LGATGAAAAT TLLPPSVHAA MAEPMRRGGL DAIEHVIVLM
QENRSFDHYY GSLRGVRGFS DTHPLELPSG RSVFEQPNPA GGTVLPFSVR KAAELAGRKP
DDIQYLGDLD HSWNGSGKAW ARGWNNGWIA AKTPATMTYY ERRDIALQYE LADTFTICDA
YHCSIFGSTN PNRNFLWTGT TGFEPGSTTN RAVTNAAYSY DHQGYDWTTY PERLEAAGVP
WQIYQEWDNF TDNAVEYFVP FKKVGTKILA SVEEKFRTTE EFYDALPKKT PEERAKLLAQ
FDAGVAKLTP AERNLFKKAM YRSEPETLVT RLKADIQARR LPAVSWLVPS AKDSEHPGAS
TPVGSANLIY RVLDALASDR ETWSKTVLLI NFDENDGYFD HVPPPMPPGN AANDADHFNG
QPLGFGPRVP MTVVSPWSIG GNVDSTVYDH TSVLRFLERW TGVAEPNISK WRRTVAGDLT
GAFDFSRAGR QPRVNRPGPV PAPISRWRPS APAEQSLPVA EPGNRPSRPL PYQVSVSGSV
DKSGNLALSL ANSGSSSAHF ALYPYKGEFA EPAHRDVRGE APEVVRLAGD EYRVVVQGPN
RSWWELRGNR KGAAAGVDVR TRFLTWRSGV EFKLSNSGTS ALTLRLSSSR FTRVVRVGAG
RSVTVDWPVS GGWYDVKVTA DGDPSFLRTL TARVENGRPG VSC
//