HLYC2_ECOLX
ID HLYC2_ECOLX Reviewed; 174 AA.
AC P09985;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Protein-lysine myristoyltransferase HlyC {ECO:0000305};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:P06736};
DE AltName: Full=Hemolysin C;
DE AltName: Full=Hemolysin-activating lysine-acyltransferase HlyC {ECO:0000305};
DE AltName: Full=Toxin-activating protein C, 2001 {ECO:0000303|PubMed:3894051};
GN Name=hlyC {ECO:0000303|PubMed:3894051};
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=2001;
RX PubMed=3894051; DOI=10.1016/0014-5793(85)81272-2;
RA Nicaud J.-M., Mackman N., Gray L., Holland I.B.;
RT "Characterisation of HlyC and mechanism of activation and secretion of
RT haemolysin from E. coli 2001.";
RL FEBS Lett. 187:339-344(1985).
CC -!- FUNCTION: Protein-lysine myristoyltransferase that catalyzes
CC myristoylation of the protoxin (HlyA) at two internal lysine residues,
CC thereby converting it to the active toxin.
CC {ECO:0000250|UniProtKB:P06736}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + tetradecanoyl-[ACP] = H(+) + holo-[ACP] +
CC N(6)-tetradecanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:70611,
CC Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:15437, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78477, ChEBI:CHEBI:141129;
CC Evidence={ECO:0000250|UniProtKB:P06736};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70612;
CC Evidence={ECO:0000250|UniProtKB:P06736};
CC -!- ACTIVITY REGULATION: The acyltransferase activity is inhibited by heme.
CC {ECO:0000250|UniProtKB:P06736}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P06736}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06736}.
CC -!- PTM: Proteolytically cleaved by the protease systems ClpAP, ClpXP and
CC FtsH, leading to its degradation. {ECO:0000250|UniProtKB:P06736}.
CC -!- SIMILARITY: Belongs to the RTX toxin acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; X02768; CAA26545.1; -; Genomic_DNA.
DR AlphaFoldDB; P09985; -.
DR SMR; P09985; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0009404; P:toxin metabolic process; IEA:InterPro.
DR InterPro; IPR003996; RTX_toxin-activating_protC_bac.
DR Pfam; PF02794; HlyC; 1.
DR PRINTS; PR01489; RTXTOXINC.
PE 3: Inferred from homology;
KW Acyltransferase; Cytolysis; Cytoplasm; Heme; Hemolysis; Iron;
KW Metal-binding; Transferase; Virulence.
FT CHAIN 1..174
FT /note="Protein-lysine myristoyltransferase HlyC"
FT /id="PRO_0000217877"
FT ACT_SITE 23
FT /evidence="ECO:0000250|UniProtKB:P55132"
FT ACT_SITE 92
FT /evidence="ECO:0000250|UniProtKB:P55132"
FT BINDING 151
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:P06736"
SQ SEQUENCE 174 AA; 20361 MW; 7C5E402C72284A99 CRC64;
MNINKPLEIL GHVSWLWASS PLHRNWPVSL FAINVLPAIR ANQYVLLTRD NYPVAYCSWA
NLSLENEIKY LNDVTSLVAE DWTSGDRKWF IDWIAPFGDN GALYKYMRKK FPDELFLAIR
VDPKTHVGKV SEFHGGKIDK HLANKIFKQY HHELITEVKN KTDFQFFINR LRGN
