ID A0A1M5TB03_9ACTN Unreviewed; 679 AA.
AC A0A1M5TB03;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=phospholipase C {ECO:0000256|ARBA:ARBA00012018};
DE EC=3.1.4.3 {ECO:0000256|ARBA:ARBA00012018};
GN ORFNames=SAMN05443575_3956 {ECO:0000313|EMBL:SHH47881.1};
OS Jatrophihabitans endophyticus.
OC Bacteria; Actinomycetota; Actinomycetes; Jatrophihabitantales;
OC Jatrophihabitantaceae; Jatrophihabitans.
OX NCBI_TaxID=1206085 {ECO:0000313|EMBL:SHH47881.1, ECO:0000313|Proteomes:UP000186132};
RN [1] {ECO:0000313|EMBL:SHH47881.1, ECO:0000313|Proteomes:UP000186132}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45627 {ECO:0000313|EMBL:SHH47881.1,
RC ECO:0000313|Proteomes:UP000186132};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQVU01000006; SHH47881.1; -; Genomic_DNA.
DR RefSeq; WP_073392145.1; NZ_FQVU01000006.1.
DR AlphaFoldDB; A0A1M5TB03; -.
DR STRING; 1206085.SAMN05443575_3956; -.
DR OrthoDB; 4181857at2; -.
DR Proteomes; UP000186132; 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; 2.
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 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 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:UP000186132};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 499..580
FT /note="Bacterial phospholipase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05506"
FT DOMAIN 595..663
FT /note="Bacterial phospholipase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05506"
FT REGION 462..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 679 AA; 74676 MW; 2DB7CD693F30142D CRC64;
MSELDRRRFL QLAGGGLAAS ALAQTFGESI ARAAAIPASR RHGSLRDVEH IVVLMQENRS
FDHYLGTMRG VRGFGDPHPA VLPSGRSVWH QSDGTREVLP YRPDHDDLGM AFLEGTPHGW
PDTHEAFHDG HYDRFVPAKT QTTMTHLRRG DMPFQFALGD AFTVCDGYHC STMTSTDPNR
YYMWTGWVGN DGAGKGPVVT NAEAGYAWTT YPERLERAGV SWKIYQDVGT GLDAAGSWGW
TDDAYIGNYG DNSLLYFDNY RNARPGDALY EKARRGTNAA AGDGYFDILR ADVAAGRLPQ
ISWIAAPEAF CEHPNWPVNY GAWYVSQVLD ALTSDPDVWS KTVLLVTYDE NDGYFDHVVP
PYPNTDQLAG ASTVPTVDEV YRGTEFAPAP YGLGQRVPMF VVSPWSTGGW VCSETFDHTS
IIRLMEARFG VREPNITPWR RAVCGDLTSA FDFSRHRAAA PDLPSTAGYR PPDRARHDSF
VPVPPEPGRL PSQEAGVRPS RPLGYRLDVS ATVRDDGLAL AMRNAGRLGV HLQARSQTGA
APVSFTVGAK DSLTASLPVS GRYDIALHGP HGFFRRFAGD AADVDTEAWV TTHGDRIELV
LVNRGRAAVT FRVADAYGRA RTVRVRGRDR VGVRVSTERQ HGWYDLTVTH PGTDGFRRAM
AGRVETGRPS VSDPQLSGR
//