RTXC_KINKI
ID RTXC_KINKI Reviewed; 167 AA.
AC A1YKW8;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Protein-lysine myristoyltransferase RtxC {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:32461253, ECO:0000305|PubMed:30405113};
GN Name=rtxC {ECO:0000303|PubMed:17098895};
OS Kingella kingae.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Kingella.
OX NCBI_TaxID=504;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=269-492;
RX PubMed=17098895; DOI=10.1128/jb.01319-06;
RA Kehl-Fie T.E., St Geme J.W. III;
RT "Identification and characterization of an RTX toxin in the emerging
RT pathogen Kingella kingae.";
RL J. Bacteriol. 189:430-436(2007).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=30405113; DOI=10.1038/s41426-018-0179-x;
RA Osickova A., Balashova N., Masin J., Sulc M., Roderova J., Wald T.,
RA Brown A.C., Koufos E., Chang E.H., Giannakakis A., Lally E.T., Osicka R.;
RT "Cytotoxic activity of Kingella kingae RtxA toxin depends on post-
RT translational acylation of lysine residues and cholesterol binding.";
RL Emerg. Microbes Infect. 7:178-178(2018).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=32461253; DOI=10.1074/jbc.ra120.014122;
RA Osickova A., Khaliq H., Masin J., Jurnecka D., Sukova A., Fiser R.,
RA Holubova J., Stanek O., Sebo P., Osicka R.;
RT "Acyltransferase-mediated selection of the length of the fatty acyl chain
RT and of the acylation site governs activation of bacterial RTX toxins.";
RL J. Biol. Chem. 295:9268-9280(2020).
CC -!- FUNCTION: Protein-lysine myristoyltransferase that catalyzes
CC myristoylation of the protoxin (RtxA) at two internal lysine residues,
CC thereby converting it to the active toxin.
CC {ECO:0000269|PubMed:30405113, ECO:0000269|PubMed:32461253}.
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:0000269|PubMed:32461253, ECO:0000305|PubMed:30405113};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70612;
CC Evidence={ECO:0000269|PubMed:32461253, ECO:0000305|PubMed:30405113};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RTX toxin acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; EF067866; ABK58602.1; -; Genomic_DNA.
DR RefSeq; WP_026036190.1; NZ_UGJI01000001.1.
DR EnsemblBacteria; CRZ19292; CRZ19292; KKKWG1_0116.
DR EnsemblBacteria; CRZ19497; CRZ19497; KKKWG1_0322.
DR GeneID; 61308781; -.
DR KEGG; kki:KKKWG1_0116; -.
DR KEGG; kki:KKKWG1_0322; -.
DR OrthoDB; 1823499at2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0018030; F:peptidyl-lysine N6-myristoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0009404; P:toxin metabolic process; IEA:UniProtKB-UniRule.
DR InterPro; IPR003996; RTX_toxin-activating_protC_bac.
DR Pfam; PF02794; HlyC; 1.
DR PRINTS; PR01489; RTXTOXINC.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Transferase; Virulence.
FT CHAIN 1..167
FT /note="Protein-lysine myristoyltransferase RtxC"
FT /id="PRO_0000455663"
FT ACT_SITE 20
FT /evidence="ECO:0000250|UniProtKB:P55132"
FT ACT_SITE 89
FT /evidence="ECO:0000250|UniProtKB:P55132"
SQ SEQUENCE 167 AA; 19406 MW; 66B118804802C3CD CRC64;
MDKFSELGSI AWLWTNSELH QNWPLSLFST NVIPAIETQQ YVLLVRDGMP IAYCSWARLN
LETEVKYIND VTSLKLEDWQ SGDRYWFIDW IAPFGDSYLL TKHMRKLFSD GLFRAIRVDA
GSPNGKISEF YGRNVDAKLA MQSFEQYQKE LMNALSQQDN FIISTSK
