ID W5W3A9_9PSEU Unreviewed; 464 AA.
AC W5W3A9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=phospholipase C {ECO:0000256|ARBA:ARBA00012018};
DE EC=3.1.4.3 {ECO:0000256|ARBA:ARBA00012018};
GN ORFNames=KALB_2304 {ECO:0000313|EMBL:AHH95673.1};
OS Kutzneria albida DSM 43870.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHH95673.1, ECO:0000313|Proteomes:UP000019225};
RN [1] {ECO:0000313|EMBL:AHH95673.1, ECO:0000313|Proteomes:UP000019225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43870 {ECO:0000313|EMBL:AHH95673.1};
RX PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA Bechthold A., Kalinowski J., Luzhetskyy A.;
RT "Complete genome sequence of producer of the glycopeptide antibiotic
RT Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT of Pseudonocardiaceae.";
RL BMC Genomics 15:885-885(2014).
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; CP007155; AHH95673.1; -; Genomic_DNA.
DR RefSeq; WP_030109293.1; NZ_CP007155.1.
DR AlphaFoldDB; W5W3A9; -.
DR STRING; 1449976.KALB_2304; -.
DR KEGG; kal:KALB_2304; -.
DR PATRIC; fig|1449976.3.peg.2303; -.
DR eggNOG; COG3511; Bacteria.
DR HOGENOM; CLU_008770_0_0_11; -.
DR OrthoDB; 4181857at2; -.
DR Proteomes; UP000019225; Chromosome.
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; 1.
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 PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Hydrolase {ECO:0000313|EMBL:AHH95673.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019225};
KW Secreted {ECO:0000256|ARBA:ARBA00022512}; Signal {ECO:0000256|SAM:SignalP};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..464
FT /note="phospholipase C"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038980151"
FT REGION 435..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..464
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 464 AA; 51499 MW; A55469FA47029C03 CRC64;
MLTRRRVLAA GAAAALGAMV LPGNLRRALA DTPATARGGL RDIEHVVILM QENRSFDHYF
GTMPGVRGFA DPTAMRLPNG DSVFQQPYSG HPDGYLLPFR YDTAVTSAQE TPGLPHDWND
QHSAWNGGRM DNWIKAKGAN SMAYYTREDI PFHHALAEAF TVCDNYFCSV LGPTNPNRLY
MWSGWIDPQG TAGGPAYHNY MSSANPVLSW ETYPERLTRA GVSWQVYQEE DNYDDNALAW
FRQFAEAPKS SPLYRNGMVK RSAGWFEHDA RTGRLPQVSW LVAPSAQTEH PNWMPAAGAQ
YIASKLDAIA ANPDLWAKTV FILTYDENDG YFDHVPPPTP PAGTPDEFVR GVPIGLGFRV
PTVIVSPWTA GGYVCSEALD HSSLVRFLER RFGVAEPHIS AWRRAAVGDM TSAFRFAKPA
RFPRDNAQLR YAATVSKLRQ AQQQVRDNPP PHPPTGPQRQ PGQG
//
