ID J2K0Q2_9ACTN Unreviewed; 475 AA.
AC J2K0Q2;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=phospholipase C {ECO:0000256|ARBA:ARBA00012018};
DE EC=3.1.4.3 {ECO:0000256|ARBA:ARBA00012018};
GN ORFNames=SU9_015340 {ECO:0000313|EMBL:QTZ92685.1}, SU9_16192
GN {ECO:0000313|EMBL:EJJ05970.1};
OS Streptomyces auratus AGR0001.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1160718 {ECO:0000313|EMBL:EJJ05970.1};
RN [1] {ECO:0000313|EMBL:EJJ05970.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AGR0001 {ECO:0000313|EMBL:EJJ05970.1};
RX PubMed=22965094; DOI=10.1128/JB.01155-12;
RA Han X., Li M., Ding Z., Zhao J., Ji K., Wen M., Lu T.;
RT "Genome Sequence of Streptomyces auratus Strain AGR0001, a Phoslactomycin-
RT Producing Actinomycete.";
RL J. Bacteriol. 194:5472-5473(2012).
RN [2] {ECO:0000313|EMBL:QTZ92685.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AGR0001 {ECO:0000313|EMBL:QTZ92685.1};
RA Wen M.-L., Han X.-L., Xiong J.;
RL Submitted (APR-2021) 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; AJGV01000096; EJJ05970.1; -; Genomic_DNA.
DR EMBL; CP072931; QTZ92685.1; -; Genomic_DNA.
DR RefSeq; WP_006604781.1; NZ_CP072931.1.
DR AlphaFoldDB; J2K0Q2; -.
DR STRING; 1160718.SU9_16192; -.
DR KEGG; sauh:SU9_015340; -.
DR PATRIC; fig|1160718.3.peg.3274; -.
DR eggNOG; COG3511; Bacteria.
DR HOGENOM; CLU_008770_0_0_11; -.
DR OrthoDB; 4181857at2; -.
DR Proteomes; UP000009036; 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; IPR007312; Phosphoesterase.
DR InterPro; IPR006311; TAT_signal.
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 Reference proteome {ECO:0000313|Proteomes:UP000009036};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT REGION 448..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 52732 MW; 7D7479455D7D8423 CRC64;
MPDMTRRRLL GSAAGAVGGA AALSLLPPSV QKAVAAGPAR HGSLHDVEHV VMLMQENRSF
DHYFGTLRGV RGFADPKALT LPDGRSVFHQ PDAQNPDGYL LPFRLNTHTS SAQAIPSTSH
AWSVQHEAWN GGKMDRWLPA HRKADGVNGP YVMGYHTRED IPFQFALAES FTLCDNYFCS
VFGPTWPNRL YWMTGTLDPG GTRGGPVLNN TAPKAYRWTT YAERLEAAGI SWKVYQEEDD
YGCNLLEQFQ TFRDSQPGQP LYERGMRPQP AGTFEDDARA DRLPAVSWLI PTSHQSEHPD
YLPAAGADYV AQKIEAIASN PKVWAKTVFI LNYDENDGLF DHVPPPVPPP GTKDEFVKGL
PIGGGFRVPC LIISPWTVGG WAAGEAFDHT SVLQFLERWT GVAEPNISDW RRSAFGDLTS
AFGFRHAARR PPRLPDDTAE QLAEAQWEVA HLPKPTLPGA DQHPPRQERG RRRRR
//
