ID B1VT12_STRGG Unreviewed; 688 AA.
AC B1VT12;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=phospholipase C {ECO:0000256|ARBA:ARBA00012018};
DE EC=3.1.4.3 {ECO:0000256|ARBA:ARBA00012018};
GN OrderedLocusNames=SGR_887 {ECO:0000313|EMBL:BAG17716.1};
OS Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG17716.1, ECO:0000313|Proteomes:UP000001685};
RN [1] {ECO:0000313|EMBL:BAG17716.1, ECO:0000313|Proteomes:UP000001685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX PubMed=18375553; DOI=10.1128/JB.00204-08;
RA Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA Yamashita A., Hattori M., Horinouchi S.;
RT "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT griseus IFO 13350.";
RL J. Bacteriol. 190:4050-4060(2008).
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; AP009493; BAG17716.1; -; Genomic_DNA.
DR RefSeq; WP_012378147.1; NC_010572.1.
DR AlphaFoldDB; B1VT12; -.
DR GeneID; 6209858; -.
DR KEGG; sgr:SGR_887; -.
DR PATRIC; fig|455632.4.peg.877; -.
DR eggNOG; COG3511; Bacteria.
DR HOGENOM; CLU_008770_1_0_11; -.
DR Proteomes; UP000001685; Chromosome.
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 Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 497..582
FT /note="Bacterial phospholipase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05506"
FT DOMAIN 594..672
FT /note="Bacterial phospholipase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05506"
FT REGION 452..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 688 AA; 74264 MW; 396170B4C0764275 CRC64;
MADMNRRRFL RVAGATAGFA ALSGSIDRAA AIPAHRASGT LRDVEHIVVL MQENRSFDHY
FGALKGVRGF GDPRPVTLPS GKSVWHQADA AGKETLPFHP TADDLGMQFL QGLNHDWAGG
HQAYHDGRYD RWIPAKTPTT MAYLTREDIP FHYALADRFT VCDAYHCSFI GATDPNRYYL
WSGHTGNDGT GGGPVLGNEE RGYGWTTYPE RLEEAGVSWK IYQDIGDGLD GPGGWGWIDD
AYRGNYGDNS LLYFDAYRNA RPGNPLYDKA RTGTNVAAGD DYFDGIAADV KNGKLPQISW
VAAPEAFTEH ANFPSNYGAW YIARLLDALT SDPEVWSRTA LFITYDENDG FFDHVVPPYP
PTSADQGLST ADTSTEVYAG GASYGPGVYG LGPRVPMLVV SPWSTGGYVC SETFDHTSVL
RFMERRFGVR EPNISPWRRA VCGDLTSAFD FARTEPAPGD LPDTSAYEPP DRERHPDYRP
TPPAAGSLPK QEPGSRPTRP LPYAPYVDGA VDVGTGKITL TFSPGTAAGA QFHVTSGNRT
DAPWTYTAEA GRTVSDAWNS AYSGGSHDLT VHGPNGFLRT FRSPGSAVGP EVTARHNDGS
GNLDLTLTNR GATEVRLTLS NAGAYGGGER SVTVRPGATV SRTVDLRAGK RWYDVSVTAE
GDPAFLRRFA GHVETGAAGV SDPATATG
//
