RTX1C_ACTPL
ID RTX1C_ACTPL Reviewed; 172 AA.
AC P55132;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=RTX-I toxin-activating lysine-acyltransferase ApxIC;
DE EC=2.3.1.- {ECO:0000269|PubMed:26016525};
DE AltName: Full=APX-IC;
DE AltName: Full=Cytolysin IC;
DE Short=CLY-IC;
DE AltName: Full=HLY-IC;
DE AltName: Full=RTX-I toxin determinant C;
DE AltName: Full=Toxin RTX-I-activating protein C;
GN Name=apxIC {ECO:0000303|PubMed:8181764};
GN Synonyms=apxC {ECO:0000303|PubMed:26016525}, clyIC, hlyIC;
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=ATCC 27088 / DSM 13472 / CCM 5869 / S4074 / Serotype 1;
RX PubMed=8181764; DOI=10.1016/0378-1119(94)90361-1;
RA Frey J., Haldimann A., Nicolet J., Boffini A., Prentki P.;
RT "Sequence analysis and transcription of the apxI operon (hemolysin I) from
RT Actinobacillus pleuropneumoniae.";
RL Gene 142:97-102(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate CVI 13261 / Serotype 9;
RX PubMed=8359891; DOI=10.1128/iai.61.9.3688-3695.1993;
RA Jansen R., Briaire J., Kamp E.M., Gielkens A.L.J., Smits M.A.;
RT "Structural analysis of the Actinobacillus pleuropneumoniae-RTX-toxin I
RT (ApxI) operon.";
RL Infect. Immun. 61:3688-3695(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27088 / DSM 13472 / CCM 5869 / S4074 / Serotype 1;
RA Chin N., Frey J., Chang C.F., Chang Y.-F.;
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0007744|PDB:4WHN}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 2-172, FUNCTION, CATALYTIC
RP ACTIVITY, SUBUNIT, AND MUTAGENESIS OF GLY-12; ALA-15; ALA-19; SER-21;
RP HIS-24; ASN-35; CYS-58; ASP-93 AND ARG-121.
RX PubMed=26016525; DOI=10.1073/pnas.1503832112;
RA Greene N.P., Crow A., Hughes C., Koronakis V.;
RT "Structure of a bacterial toxin-activating acyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E3058-E3066(2015).
CC -!- FUNCTION: Protein-lysine acyltransferase that catalyzes fatty acylation
CC of the protoxin, thereby converting it to the active toxin.
CC {ECO:0000269|PubMed:26016525}.
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:0000269|PubMed:26016525};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70668;
CC Evidence={ECO:0000269|PubMed:26016525};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:26016525}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RTX toxin acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; X68595; CAA48585.1; -; Genomic_DNA.
DR EMBL; X73117; CAA51547.1; -; Genomic_DNA.
DR EMBL; U05042; AAB05033.1; -; Genomic_DNA.
DR EMBL; U04954; AAB17219.1; -; Genomic_DNA.
DR PIR; I39644; I39644.
DR RefSeq; WP_009875272.1; NZ_CP030753.1.
DR PDB; 4WHN; X-ray; 2.15 A; A/B/C/D=2-172.
DR PDBsum; 4WHN; -.
DR AlphaFoldDB; P55132; -.
DR SMR; P55132; -.
DR STRING; 228399.appser1_15250; -.
DR GeneID; 66258127; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016410; F:N-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0009404; P:toxin metabolic process; IDA:UniProtKB.
DR InterPro; IPR003996; RTX_toxin-activating_protC_bac.
DR Pfam; PF02794; HlyC; 1.
DR PRINTS; PR01489; RTXTOXINC.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytolysis; Cytoplasm; Hemolysis;
KW Transferase.
FT CHAIN 1..172
FT /note="RTX-I toxin-activating lysine-acyltransferase ApxIC"
FT /id="PRO_0000217883"
FT ACT_SITE 24
FT /evidence="ECO:0000305|PubMed:26016525"
FT ACT_SITE 93
FT /evidence="ECO:0000305|PubMed:26016525"
FT MUTAGEN 12
FT /note="G->A: Does not affect homodimerization."
FT /evidence="ECO:0000269|PubMed:26016525"
FT MUTAGEN 12
FT /note="G->E: Abolished homodimerization."
FT /evidence="ECO:0000269|PubMed:26016525"
FT MUTAGEN 15
FT /note="A->E: Abolished homodimerization."
FT /evidence="ECO:0000269|PubMed:26016525"
FT MUTAGEN 19
FT /note="A->E: Does not affect homodimerization."
FT /evidence="ECO:0000269|PubMed:26016525"
FT MUTAGEN 21
FT /note="Missing: Slightly reduced ability to activate the
FT protoxin."
FT /evidence="ECO:0000269|PubMed:26016525"
FT MUTAGEN 24
FT /note="H->A: Strongly reduced protein-lysine
FT acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:26016525"
FT MUTAGEN 35
FT /note="N->A: Strongly reduced protein-lysine
FT acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:26016525"
FT MUTAGEN 58
FT /note="C->A: Does not affect the protein-lysine
FT acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:26016525"
FT MUTAGEN 93
FT /note="D->A: Abolished protein-lysine acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:26016525"
FT MUTAGEN 121
FT /note="R->A: Abolished protein-lysine acyltransferase
FT activity. Abolished binding to acyl-CoA."
FT /evidence="ECO:0000269|PubMed:26016525"
FT HELIX 3..19
FT /evidence="ECO:0007829|PDB:4WHN"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:4WHN"
FT HELIX 29..42
FT /evidence="ECO:0007829|PDB:4WHN"
FT STRAND 45..63
FT /evidence="ECO:0007829|PDB:4WHN"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:4WHN"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:4WHN"
FT STRAND 87..95
FT /evidence="ECO:0007829|PDB:4WHN"
FT HELIX 101..111
FT /evidence="ECO:0007829|PDB:4WHN"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:4WHN"
FT STRAND 124..135
FT /evidence="ECO:0007829|PDB:4WHN"
FT HELIX 141..163
FT /evidence="ECO:0007829|PDB:4WHN"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:4WHN"
SQ SEQUENCE 172 AA; 19895 MW; 3CBFEE2B868AD65E CRC64;
MSKKINGFEV LGEVAWLWAS SPLHRKWPLS LLAINVLPAI ESNQYVLLKR DGFPIAFCSW
ANLNLENEIK YLDDVASLVA DDWTSGDRRW FIDWIAPFGD SAALYKHMRD NFPNELFRAI
RVDPDSRVGK ISEFHGGKID KKLASKIFQQ YHFELMSELK NKQNFKFSLV NS
