HLYC1_ECOLX
ID HLYC1_ECOLX Reviewed; 170 AA.
AC P09984;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 66.
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, J96;
GN Name=hlyC {ECO:0000303|PubMed:3891743};
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=J96 / Serotype O4;
RX PubMed=3891743; DOI=10.1128/jb.163.1.94-105.1985;
RA Felmlee T., Pellett S., Welch R.A.;
RT "Nucleotide sequence of an Escherichia coli chromosomal hemolysin.";
RL J. Bacteriol. 163:94-105(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; M10133; AAA23974.1; -; Genomic_DNA.
DR PIR; C24433; LEECC.
DR AlphaFoldDB; P09984; -.
DR SMR; P09984; -.
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..170
FT /note="Protein-lysine myristoyltransferase HlyC"
FT /id="PRO_0000217876"
FT ACT_SITE 23
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 170 AA; 19726 MW; 0A854A23FA309DB9 CRC64;
MNRNNPLEVL GHVSWLWASS PLHRNWPVSL FAINVLPAIR ANQYALLTRD NYPVAYCSWA
NLSLENEIKY LNDVTSLVAE DWTSGDRKWF IVWIAPFGDN GALYKYMRKK FPDELFRAIR
VDPKTHVGKV SEFHGGKIDK QLANKIFKQY HHELITEVKN KSDFNFSLTG
