ID A0A0M2HT88_9MICO Unreviewed; 581 AA.
AC A0A0M2HT88;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=phospholipase C {ECO:0000256|ARBA:ARBA00012018};
DE EC=3.1.4.3 {ECO:0000256|ARBA:ARBA00012018};
GN Name=plcB {ECO:0000313|EMBL:KJL48135.1};
GN ORFNames=RS84_01764 {ECO:0000313|EMBL:KJL48135.1};
OS Microbacterium hydrocarbonoxydans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=273678 {ECO:0000313|EMBL:KJL48135.1, ECO:0000313|Proteomes:UP000033900};
RN [1] {ECO:0000313|EMBL:KJL48135.1, ECO:0000313|Proteomes:UP000033900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA35 {ECO:0000313|EMBL:KJL48135.1,
RC ECO:0000313|Proteomes:UP000033900};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) 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:KJL48135.1}.
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DR EMBL; JYJB01000008; KJL48135.1; -; Genomic_DNA.
DR RefSeq; WP_045257378.1; NZ_JYJB01000008.1.
DR AlphaFoldDB; A0A0M2HT88; -.
DR STRING; 273678.RS84_01764; -.
DR PATRIC; fig|273678.4.peg.1768; -.
DR OrthoDB; 4181857at2; -.
DR Proteomes; UP000033900; Unassembled WGS sequence.
DR GO; GO:0034480; F:phosphatidylcholine phospholipase C activity; IEA:UniProtKB-EC.
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:SF1; NON-SPECIFIC PHOSPHOLIPASE C1; 1.
DR PANTHER; PTHR31956; NON-SPECIFIC PHOSPHOLIPASE C4-RELATED; 1.
DR Pfam; PF04185; Phosphoesterase; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Hydrolase {ECO:0000313|EMBL:KJL48135.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033900};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT REGION 507..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 581 AA; 62715 MW; 09211738F8690C9D CRC64;
MAEHDSPGGT DRRGFLKLGG AAVAGAVIGG AGGAAIGASL AGDHDGGFAQ EPDPFAALTP
RSEPGFDHVV VLMGENRSFD NLLGYLYTPQ SLPAGERFEG LAFGAHSNTA PDGTVVEAHV
YQGATDRIMS LPDPDPGEEY PHVNTQIFGT IDPPGNSELY IDQMSAPFNA PPRGAKADMS
GFLKDYIVNF RRLRRGVEPR AEEAAHIMGS FSPEMLPVLS TLAAEFAVFD HWYAAVPSQT
FCNRSFFHAS TSHGFVTNVG GGGYRKWLDA PAAPTVFNRL EDAGLTWRIY FDELQLVSFT
GLLHAGALEK YWRTDHFGTM ADFYSDAENG TLPAYAFIEP RMVYDHNDFH PPFGVLREGE
ADGEPVLDSA ISDVRAGDRL VHDVYEAIRT SASPHGSNAI NTLLLITFDE HGGCYDHVPP
PEATTPTAAS GEGEMGFTFN RLGCRVPAIA VSAYTKRGTI IHDEMHHGSV TATLSRLHGL
KPLNDRDASA NTLLDVVNLD RPRHPSDWPV TVPAYTPPNP EQAPPGDADR AKPLTPPARG
LLGLLIARYG RPDEPEPETF ADAYRLLHEH GEELFGPPKG N
//
