ID E3HYA3_ACHXA Unreviewed; 233 AA.
AC E3HYA3;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Type IV leader peptidase family protein 2 {ECO:0000313|EMBL:ADP20057.1};
GN OrderedLocusNames=AXYL_06775 {ECO:0000313|EMBL:ADP20057.1};
OS Achromobacter xylosoxidans (strain A8).
OG Plasmid pA82 {ECO:0000313|EMBL:ADP20057.1,
OG ECO:0000313|Proteomes:UP000006876}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP20057.1, ECO:0000313|Proteomes:UP000006876};
RN [1] {ECO:0000313|Proteomes:UP000006876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A8 {ECO:0000313|Proteomes:UP000006876};
RC PLASMID=pA82 {ECO:0000313|Proteomes:UP000006876};
RX PubMed=21097610; DOI=10.1128/JB.01299-10;
RA Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT "Complete genome sequence of the haloaromatic acids-degrading bacterium
RT Achromobacter xylosoxidans A8.";
RL J. Bacteriol. 193:791-792(2011).
CC -!- SIMILARITY: Belongs to the peptidase A24 family.
CC {ECO:0000256|ARBA:ARBA00005801, ECO:0000256|RuleBase:RU003793}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002289; ADP20057.1; -; Genomic_DNA.
DR RefSeq; WP_013397245.1; NC_014642.1.
DR AlphaFoldDB; E3HYA3; -.
DR KEGG; axy:AXYL_06775; -.
DR eggNOG; COG1989; Bacteria.
DR HOGENOM; CLU_1093581_0_0_4; -.
DR OrthoDB; 9789291at2; -.
DR Proteomes; UP000006876; Plasmid pA82.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR Gene3D; 1.20.120.1220; -; 1.
DR InterPro; IPR014032; Peptidase_A24A_bac.
DR InterPro; IPR000045; Prepilin_IV_endopep_pep.
DR PANTHER; PTHR30487:SF0; PREPILIN LEADER PEPTIDASE_N-METHYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR30487; TYPE 4 PREPILIN-LIKE PROTEINS LEADER PEPTIDE-PROCESSING ENZYME; 1.
DR Pfam; PF01478; Peptidase_A24; 1.
DR PRINTS; PR00864; PREPILNPTASE.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius}; Plasmid {ECO:0000313|EMBL:ADP20057.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..22
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 53..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 85..193
FT /note="Prepilin type IV endopeptidase peptidase"
FT /evidence="ECO:0000259|Pfam:PF01478"
SQ SEQUENCE 233 AA; 23971 MW; F4E66FFA64C8F82D CRC64;
MTTPITLAAM AVVGIGAGEA VLRLRQRMER ILDAECYPGA TLQMLFAGGF RPVAGGLAVR
ATLLAIWIAC AIAPLAPANT VALAFFLTML AAGAFVDANS QVLPDEITGS LVWGGLIAQW
AGIVPWGGSI ETAVIGVVAG YGAIWLVTAG YCVCRRMAAI GHGDLKMIAG LSAWLGVGEL
PAVILGSCVL QVFAQLVMRR GGTMAFGPAL AITGAILAIL KLAGIELPFL RLL
//
