ID A0A1G9N3I6_9ACTN Unreviewed; 654 AA.
AC A0A1G9N3I6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=phospholipase C {ECO:0000256|ARBA:ARBA00012018};
DE EC=3.1.4.3 {ECO:0000256|ARBA:ARBA00012018};
GN ORFNames=SAMN05421869_13112 {ECO:0000313|EMBL:SDL80425.1};
OS Nonomuraea jiangxiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=633440 {ECO:0000313|EMBL:SDL80425.1, ECO:0000313|Proteomes:UP000199202};
RN [1] {ECO:0000313|EMBL:SDL80425.1, ECO:0000313|Proteomes:UP000199202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.6533 {ECO:0000313|EMBL:SDL80425.1,
RC ECO:0000313|Proteomes:UP000199202};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNDJ01000031; SDL80425.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9N3I6; -.
DR STRING; 633440.SAMN05421869_13112; -.
DR OrthoDB; 4181857at2; -.
DR Proteomes; UP000199202; 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 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; IPR008475; PLipase_C_C.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR03396; PC_PLC; 1.
DR NCBIfam; TIGR01409; TAT_signal_seq; 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 Pfam; PF05506; PLipase_C_C; 2.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Reference proteome {ECO:0000313|Proteomes:UP000199202};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 468..555
FT /note="Bacterial phospholipase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05506"
FT DOMAIN 582..649
FT /note="Bacterial phospholipase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05506"
FT REGION 446..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 654 AA; 72226 MW; 8B740603DCA70751 CRC64;
MTEFSRRTFI GATAAAGAAA AVVGLPDTAQ AAKRGSIDEV KHVVILMQEN RSFDHYFGNL
NGVRGFGDRQ ALVLPNGEPV FHQPDRGRAE GHLLPFRMDT TKYNAQNAGG LPHDWSSGHV
AVNNGAMDKW VNAKGERTMG YFTREDIPYQ YALADAFTLC DGYFCSLNGP TDPNRLYLWS
GTAGPGRDGT TGPWTDNTPV TDNPVADWTT YAERLETAGV SWRVYHNPSK DEREGDYDDN
GLSYFRQFHA FPKDDPRYVN AMTKFDLTAF DQHCKDGTLP TVSWLVAPYL FCEHPDASPD
YGAHWVNTAL QSLFANPDVW RHTVFLVMYD ENDGYFDHVI PPMPEPGTPE EFVGDKPIGL
GSRVPLFVIS PFSRGGWVNS QVFDHTSVLR FLEQVTGVQE PNISAWRRAV CGDLTSCFDF
GKPDYSIPGL PDTVELMARA DANHSLPPVQ VPRSGEQQMP VPEQGDRPHR PLPYRPWADV
TVDRATGEVT CTFTNDGPVA FHFTMLPNIV LPATGTPFTV APRSSRTYVW DAAATDGRYD
FSVYGADGFV RRFAGTVVRD GQDDVAVPSV RAKLRGGRPD SASIEVTLVN DGETEVSFRL
TPNDFGGRPK TVWVKPGARA EATWPVENGR YDFTVTAGTG TRFAQRYAGT VHQV
//
