ID A3N1F8_ACTP2 Unreviewed; 504 AA.
AC A3N1F8;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Putative zinc protease {ECO:0000313|EMBL:ABN74244.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:ABN74244.1};
GN OrderedLocusNames=APL_1154 {ECO:0000313|EMBL:ABN74244.1};
OS Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=416269 {ECO:0000313|EMBL:ABN74244.1, ECO:0000313|Proteomes:UP000001432};
RN [1] {ECO:0000313|EMBL:ABN74244.1, ECO:0000313|Proteomes:UP000001432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L20 {ECO:0000313|EMBL:ABN74244.1,
RC ECO:0000313|Proteomes:UP000001432};
RX PubMed=18065534; DOI=10.1128/JB.01845-07;
RA Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA Nash J.H.;
RT "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT (serotype 5b).";
RL J. Bacteriol. 190:1495-1496(2008).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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DR EMBL; CP000569; ABN74244.1; -; Genomic_DNA.
DR RefSeq; WP_005601646.1; NC_009053.1.
DR AlphaFoldDB; A3N1F8; -.
DR STRING; 416269.APL_1154; -.
DR EnsemblBacteria; ABN74244; ABN74244; APL_1154.
DR GeneID; 69418392; -.
DR KEGG; apl:APL_1154; -.
DR PATRIC; fig|416269.6.peg.1203; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_536153_0_0_6; -.
DR Proteomes; UP000001432; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF34; ZINC PROTEASE PQQL-LIKE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABN74244.1};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:ABN74244.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001432};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..504
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002655603"
FT DOMAIN 46..161
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 193..374
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 474..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 504 AA; 57664 MW; D77CB7B5DFB5C38C CRC64;
MRIILTSLVL FAASTTSYAE KSEPIQGQLE NGLRYTLLPL HSEKGRIEIR MKVNAGAIDE
TDTQLGATNV LKHLVLRGTK AHPNGLTPYL NEQKWKPENN YRIESGYDHT TYHMIPPSTS
NLDKSLYLLE QMLFQAKLTQ EDLDDERKHI LEEWRQAQSV GRLMNQKRIA AVRTDSRYAD
RAIIGTAENI QNLPATQLQQ FYQTWYTPNN MQLLVVGDIE PEAAQQQIQQ RFSSFTAKEM
PKRDYLEPKL SEGLAINKLQ DARSSVSQVA YIFRFDEMKH RVRTNEARYE RLIDRLALAL
LSQRLQDQSA ALPKGVSAIT VRKSDIGRNT AALGWFATVA STQHELGLKQ IFSEIEHLKG
SPITEEELTK QKEAVQIQIE NAKKDENDRD FQQWLQIMSE SVLADKPYLT QKKLAELLEP
MLKKVSAKEV NERIQQWIGS KDRLINYQPP RKVQIKPITL ETVNKLQAEA EQTELAKTEA
EKTEVEKAEV EKTEATQPAT EKNP
//
