ID A0A1R1MBD9_9MICC Unreviewed; 565 AA.
AC A0A1R1MBD9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=phospholipase C {ECO:0000256|ARBA:ARBA00012018};
DE EC=3.1.4.3 {ECO:0000256|ARBA:ARBA00012018};
GN ORFNames=BGP79_15520 {ECO:0000313|EMBL:OMH37089.1};
OS Tersicoccus sp. Bi-70.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Tersicoccus.
OX NCBI_TaxID=1897634 {ECO:0000313|EMBL:OMH37089.1, ECO:0000313|Proteomes:UP000187343};
RN [1] {ECO:0000313|EMBL:OMH37089.1, ECO:0000313|Proteomes:UP000187343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bi-70 {ECO:0000313|EMBL:OMH37089.1,
RC ECO:0000313|Proteomes:UP000187343};
RA Nakajima Y., Yoshizawa S., Ogura Y., Hayashi T., Kogure K.;
RT "Draft genome of Tersicoccus sp. strain Bi-70.";
RL Submitted (AUG-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}.
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:OMH37089.1}.
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DR EMBL; MIEU01000002; OMH37089.1; -; Genomic_DNA.
DR RefSeq; WP_076693197.1; NZ_MIEU01000002.1.
DR AlphaFoldDB; A0A1R1MBD9; -.
DR STRING; 1897634.BGP79_15520; -.
DR Proteomes; UP000187343; Unassembled WGS sequence.
DR GO; GO:0034480; F:phosphatidylcholine phospholipase C activity; IEA:UniProtKB-EC.
DR CDD; cd16013; AcpA; 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 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 Secreted {ECO:0000256|ARBA:ARBA00022512}; Signal {ECO:0000256|SAM:SignalP};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..565
FT /note="phospholipase C"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038807613"
FT REGION 220..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 565 AA; 59401 MW; CC8BBDB701384AA5 CRC64;
MNPRRLAAAA SAVVVAGATA AGGVLGVGVP AAAASQPSTA TPIKHVVVIF GENVSFDHYF
GTYPNAANTP GETLQGSGTP AATFTAAPDT PKNINTLASA GLLAPNNPNT VQPARLSPSQ
AVTCDQDHGY TAEQEAYHGG LMDQFVQYTS RDACGTNQFG RPGLTMDYYD GNTVTGLWNY
AQHYAMSDNH FSTTFGPSTP GALNLVSGQT HGVKEFTATG QPVTPTASDY TVRQPDATGT
GTVINDPDPV YDDCSNSSHT KTNTLAGMTG RNVGDLLNAR GVSWGWFQGG FAPTTPASGT
TPAACLASHT NAAGASVVDY SPHHQPFQYY ASTANPHHLA PASTAEIGHN GRANHQYDLT
SFDSVVNTGN LPAVSFLKAG EFQDGHAAYS DPVDEQRFVT KTINTIEKSP NWKDTAVVVA
YDDSDGWYDH VAAQVKNASN SPDDAAWCQQ AATRGTPIAG GYQDRCGPGP RQPLIVVSPF
AKQNFVDHTE TDQASILRFI EDNWSTGQIG DASADATAGS LSAIFNFHHE RRDQVLLDEE
NGSVAAVLHG NHGHGDNGHG GHHHR
//
