RTX2C_ACTPL
ID RTX2C_ACTPL Reviewed; 160 AA.
AC P0A3I3; P15376; P55119;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=RTX-II toxin-activating lysine-acyltransferase ApxIIC;
DE EC=2.3.1.- {ECO:0000250|UniProtKB:P55132};
DE AltName: Full=APX-IIC;
DE AltName: Full=Cytolysin IIC;
DE Short=CLY-IIC;
DE AltName: Full=HLY-IIC;
DE AltName: Full=RTX-II toxin determinant C;
DE AltName: Full=Toxin RTX-II-activating protein C;
GN Name=apxIIC; Synonyms=appC, ashC, clyIIC, cytC, hlyC;
OS Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=715;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serotype 5;
RX PubMed=2693022; DOI=10.1089/dna.1.1989.8.635;
RA Chang Y.-F., Young R., Struck D.K.;
RT "Cloning and characterization of a hemolysin gene from Actinobacillus
RT (Haemophilus) pleuropneumoniae.";
RL DNA 8:635-647(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate CVI 13261 / Serotype 9;
RX PubMed=1937809; DOI=10.1128/iai.59.12.4497-4504.1991;
RA Smits M.A., Briaire J., Jansen R., Smith H.E., Kamp E.M., Gielkens A.L.J.;
RT "Cytolysins of Actinobacillus pleuropneumoniae serotype 9.";
RL Infect. Immun. 59:4497-4504(1991).
CC -!- FUNCTION: Protein-lysine acyltransferase that catalyzes fatty acylation
CC of the protoxin, thereby converting it to the active toxin.
CC {ECO:0000250|UniProtKB:P55132}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-[ACP] + L-lysyl-[protein] = H(+) + holo-[ACP] +
CC N(6)-(fatty acyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:70667, Rhea:RHEA-
CC COMP:9685, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14125, Rhea:RHEA-
CC COMP:17946, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:138651, ChEBI:CHEBI:189854;
CC Evidence={ECO:0000250|UniProtKB:P55132};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70668;
CC Evidence={ECO:0000250|UniProtKB:P55132};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P55132}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RTX toxin acyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA43422.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M30602; AAA87231.1; -; Genomic_DNA.
DR EMBL; X61111; CAA43422.1; ALT_INIT; Genomic_DNA.
DR PIR; A33389; A33389.
DR PIR; S18852; A43599.
DR RefSeq; WP_012263032.1; NZ_UIFY01000002.1.
DR AlphaFoldDB; P0A3I3; -.
DR SMR; P0A3I3; -.
DR GeneID; 66259877; -.
DR OMA; WLWMHSP; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; 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; Hemolysis; Transferase.
FT CHAIN 1..160
FT /note="RTX-II toxin-activating lysine-acyltransferase
FT ApxIIC"
FT /id="PRO_0000217884"
FT ACT_SITE 23
FT /evidence="ECO:0000250|UniProtKB:P55132"
FT ACT_SITE 92
FT /evidence="ECO:0000250|UniProtKB:P55132"
FT VARIANT 6
FT /note="Missing (in strain: Serotype 5)"
FT VARIANT 43..47
FT /note="QYLLL -> PIFVT (in strain: Serotype 5)"
FT VARIANT 59..60
FT /note="WA -> SR (in strain: Serotype 5)"
SQ SEQUENCE 160 AA; 18662 MW; C155726F845C1C9F CRC64;
MMLKNDFNVL GQIAWLWANS PMHRNWSVSL LMKNVIPAIE NDQYLLLVDD GFPIAYCSWA
KLTLESEARY VKDTNSLKID DWNAGDRIWI IDWIAPFGDS SLLYKHMRQR FPYDIGRAIR
IYPSKKDTGK IIYLKGGKIT KKVAEKTFLQ YEQELITALQ
