ID A0A0F0L0Z2_9MICO Unreviewed; 729 AA.
AC A0A0F0L0Z2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=phospholipase C {ECO:0000256|ARBA:ARBA00012018};
DE EC=3.1.4.3 {ECO:0000256|ARBA:ARBA00012018};
GN Name=plcN_1 {ECO:0000313|EMBL:KJL26783.1};
GN ORFNames=RL72_00839 {ECO:0000313|EMBL:KJL26783.1};
OS Microbacterium azadirachtae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=582680 {ECO:0000313|EMBL:KJL26783.1, ECO:0000313|Proteomes:UP000033448};
RN [1] {ECO:0000313|EMBL:KJL26783.1, ECO:0000313|Proteomes:UP000033448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23848 {ECO:0000313|EMBL:KJL26783.1,
RC ECO:0000313|Proteomes:UP000033448};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) 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}.
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:KJL26783.1}.
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DR EMBL; JYIT01000061; KJL26783.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0L0Z2; -.
DR PATRIC; fig|582680.7.peg.867; -.
DR OrthoDB; 4181857at2; -.
DR Proteomes; UP000033448; 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; IPR007312; Phosphoesterase.
DR InterPro; IPR008475; PLipase_C_C.
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 Pfam; PF05506; PLipase_C_C; 2.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Hydrolase {ECO:0000313|EMBL:KJL26783.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033448};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 541..630
FT /note="Bacterial phospholipase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05506"
FT DOMAIN 655..723
FT /note="Bacterial phospholipase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05506"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 729 AA; 77428 MW; 6A5FE5A36EA15B50 CRC64;
MSSEPVPFTP DPYDRPQTVP DEVLRSGMTR RGMLRALGLL GGAAAVGAGL GAGVSASSAA
AATARGGAQA AGTSRAYALP EGFSGDITDI KHVVILMQEN RSFDHYYGAL PGVRGFDDKQ
ALRFPNGTDV FSQPQGSSFV KPSRVTTVAG TTTGLDHSYS GGTSAWAGGR YNNWVGAKGA
NTMHYVSGEE IPWQYSLASA YTICDNWHCS VMGPTTPNRL YAWTGTSGGV VDNGGESNGT
RAWQTYPEAL QAAGVSWRIY VDNTNNGSSW VGDYTDNPIR GFSAFTTSGS TATDLANRGD
AAKNAPGTGL VWRAGSAPYA STGVVNNDSD ANLNGVLKDF IAACKPGAQY PLPQVSWIVA
PYSWSEHPSA NPEHGAHFSN RVIQTLQSNP DIWKSTLLIM TFDENDGYFD HVLPPFAEPG
TPGEYNGSTP IGYGARIPTI LVSPWTRGGW VGTETFDHTS LIRFLETWTT AIGTPALSTT
ITAWRRGISG DLTSAMDFAH PVIDIPSLPD TDALVQIARA GGTIGTQVPP ADKWSSTPLK
HRPLSYHPHG VFVEDRKTGK VSVQLSLVGG PSGKAVSLQA FPDRYLPFAN TPYTVSAAKP
AAHVWDATAQ DGRYAFSVYG PDGFVRSHAG TVVPAGQNGA GVPRAEVDLV AGENPTVEIS
LHNDGRQRVH FELVPNDHAG TAQRVWVKPG GTEKVTWPTD EGYYDVVITA DTGAGWRHRY
AGRVAQLPA
//