ID M3A5D8_STRMB Unreviewed; 475 AA.
AC M3A5D8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=phospholipase C {ECO:0000256|ARBA:ARBA00012018};
DE EC=3.1.4.3 {ECO:0000256|ARBA:ARBA00012018};
GN ORFNames=H340_12000 {ECO:0000313|EMBL:EMF00324.1};
OS Streptomyces mobaraensis NBRC 13819 = DSM 40847.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1223523 {ECO:0000313|EMBL:EMF00324.1, ECO:0000313|Proteomes:UP000011740};
RN [1] {ECO:0000313|EMBL:EMF00324.1, ECO:0000313|Proteomes:UP000011740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40847 {ECO:0000313|EMBL:EMF00324.1,
RC ECO:0000313|Proteomes:UP000011740};
RX PubMed=23558536;
RA Yang H., He T., Wu W., Zhu W., Lu B., Sun W.;
RT "Whole-Genome Shotgun Assembly and Analysis of the Genome of Streptomyces
RT mobaraensis DSM 40847, a Strain for Industrial Production of Microbial
RT Transglutaminase.";
RL Genome Announc. 1:E0014313-E0014313(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:EMF00324.1}.
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DR EMBL; AORZ01000029; EMF00324.1; -; Genomic_DNA.
DR RefSeq; WP_004943643.1; NZ_CP072827.1.
DR AlphaFoldDB; M3A5D8; -.
DR STRING; 1223523.H340_12000; -.
DR PATRIC; fig|1223523.3.peg.2454; -.
DR eggNOG; COG3511; Bacteria.
DR Proteomes; UP000011740; Unassembled WGS sequence.
DR GO; GO:0034480; F:phosphatidylcholine phospholipase C activity; IEA:UniProtKB-EC.
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; 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 SUPFAM; SSF53649; Alkaline phosphatase-like; 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 REGION 450..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 52883 MW; C0485A2228DD13A5 CRC64;
MPGIISRRRL LGSAAAGAGA AALSLLPPSV QRAVAAGPPR RGSLADVEHV VMLMQENRSF
DHYFGTLKGV RGFADPKALR LSTGRSVFHQ PDAENPKGYL LPFHLDTRKT SAQAIPSTSH
AWSVQHEAWN GGKMDKWLPA HRKADGKNGP YVMGYHTRED IPFQFALAET FTICDNYFCS
VFGPTWPNRL YWMTGTIDPG GTKGGPVISN TMPSPYRWTT YAERLQAAGV SWRVYQQEDN
YGCNMLEWFK RFRDAKPGDP LYERGMRRQP EGTFEDDARN DRLPAVSWII PTGPQSEHPY
FMPAAGADFV AKKIEAIADN PKVWAKTVFI LNYDENDGLF DHVPPPVPPK GTKDEFVKGL
PIGGGFRVPC LIVSPWTVGG WAAGEAFDHT SALRFLERFT GVREPNISDW RRRTFGDLTS
AFGFDAPAPR APRLPRDTAK ELEEAEWEVA HLPKPTLPGA TQKVPVQEKG TRPRR
//
