ID H0E2T2_9ACTN Unreviewed; 503 AA.
AC H0E2T2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=phospholipase C {ECO:0000256|ARBA:ARBA00012018};
DE EC=3.1.4.3 {ECO:0000256|ARBA:ARBA00012018};
GN ORFNames=PAI11_10970 {ECO:0000313|EMBL:EHN12010.1};
OS Patulibacter medicamentivorans.
OC Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC Patulibacteraceae; Patulibacter.
OX NCBI_TaxID=1097667 {ECO:0000313|EMBL:EHN12010.1, ECO:0000313|Proteomes:UP000005143};
RN [1] {ECO:0000313|EMBL:EHN12010.1, ECO:0000313|Proteomes:UP000005143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I11 {ECO:0000313|EMBL:EHN12010.1,
RC ECO:0000313|Proteomes:UP000005143};
RX PubMed=23212173; DOI=10.1007/s10532-012-9610-5;
RA Almeida B., Kjeldal H., Lolas I., Knudsen A.D., Carvalho G., Nielsen K.L.,
RA Barreto Crespo M.T., Stensballe A., Nielsen J.L.;
RT "Quantitative proteomic analysis of ibuprofen-degrading Patulibacter sp.
RT strain I11.";
RL Biodegradation 24:615-630(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 -!- 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:EHN12010.1}.
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DR EMBL; AGUD01000051; EHN12010.1; -; Genomic_DNA.
DR RefSeq; WP_007571816.1; NZ_AGUD01000051.1.
DR AlphaFoldDB; H0E2T2; -.
DR PATRIC; fig|1097667.3.peg.1095; -.
DR OrthoDB; 4181857at2; -.
DR Proteomes; UP000005143; Unassembled WGS sequence.
DR GO; GO:0034480; F:phosphatidylcholine phospholipase C activity; IEA:UniProtKB-EC.
DR CDD; cd16013; AcpA; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 2.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR007312; Phosphoesterase.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR31956:SF1; NON-SPECIFIC PHOSPHOLIPASE C1; 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:EHN12010.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005143};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT REGION 436..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 503 AA; 55715 MW; 72F52EE999642D66 CRC64;
MPDVHDPDEA ERLEAEHHDA YHSRREFLER TAAAAGLAGM GLALSPDTVL AEATRATTRA
LPSARNLPID TFVVLMMENR SFDHYLGWLP GADGRQAGLT FRDKQGKVHA THRLAPDFQG
LAYLDPDHSW EGGRKQLDGG RNDGFLQADS DVFSIGYYTK ADLPFIPHVA QAFTAYDRFF
CSLLASTYPN RYYMHSAQSY GRRDNAFPFL KADSPLGLPD STIFNALAQK GISSRYFYSD
IPVAALWGVP GLARSGAMQE YYERCAAGTL PAVSFVDPSF NGEEAGTSGD EHPHGDVRVG
QAFMSDVVHA FLKSPQYKRG ALFIVYDEWG GFFDHVRPPR VPDVRASRDV ASDFGQMGFR
IPAVAVSPWA RRGHVDHGVY GFESILKLIR YRYGLAPLTR RDQFARNIGL SFDFAHAPKL
EPPPLPTPRR IMRGAPIGAR PAATDRQARL RDGGNAPPAP ERAKPHDLAE LYTSGYLDRL
GFDYRPATPA RMFSHPSSMG LRP
//
