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Database: UniProt
Entry: A0A1M5R304_9ACTN
LinkDB: A0A1M5R304_9ACTN
Original site: A0A1M5R304_9ACTN 
ID   A0A1M5R304_9ACTN        Unreviewed;       476 AA.
AC   A0A1M5R304;
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_3430 {ECO:0000313|EMBL:SHH20754.1};
OS   Jatrophihabitans endophyticus.
OC   Bacteria; Actinomycetota; Actinomycetes; Jatrophihabitantales;
OC   Jatrophihabitantaceae; Jatrophihabitans.
OX   NCBI_TaxID=1206085 {ECO:0000313|EMBL:SHH20754.1, ECO:0000313|Proteomes:UP000186132};
RN   [1] {ECO:0000313|EMBL:SHH20754.1, ECO:0000313|Proteomes:UP000186132}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45627 {ECO:0000313|EMBL:SHH20754.1,
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; FQVU01000005; SHH20754.1; -; Genomic_DNA.
DR   RefSeq; WP_073391930.1; NZ_FQVU01000005.1.
DR   AlphaFoldDB; A0A1M5R304; -.
DR   STRING; 1206085.SAMN05443575_3430; -.
DR   OrthoDB; 4181857at2; -.
DR   Proteomes; UP000186132; Unassembled WGS sequence.
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; 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: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:UP000186132};
KW   Secreted {ECO:0000256|ARBA:ARBA00022512};
KW   Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT   REGION          428..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   476 AA;  52331 MW;  3DBAF6BDDDBC7246 CRC64;
     MPDLTRRRFL GTAAATAGAG AAMGVLPRSV QQALATTPTR RPRLRDIEHV VLLMQENRSF
     DHYYGTLSGV AGFDDRDAIR LATGRDVFHQ PDAVNPDGYL LPFHLDTEHT SAQAIPSTSH
     AWAVQHAAWN GGRMDNWLPA HRAADKANGP YVMGYYERDD IPFQFALADA FTICDHYHCS
     VMGPTWPNRL FWMSGTNDPN GDAGGPILAN TLPHGPYTWT TYAERLQRAG VSWQVYGDEA
     GMKAYNMLPN FRAFQQAAPG TPLYDRGVKA VDPGQFAYDA AHDRLPTVSW LVPGHGQSEH
     PAELPAAGAD FVARQIAAIA ANRDVWAKTL FVLDYDENDG LFDHVVPPTP RPGTPDEFVD
     GLPVGGGFRV PCILVSPWTA GGWVASEPFD HTSVLQLLEQ VTGVREPNIS AWRRRTFGDL
     TSALRLRDAT RRPPRLPDTA AQLAKAQDEV ATSPAPELPG ARQRRPHQER GHRPHV
//
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