ID A3N3H7_ACTP2 Unreviewed; 982 AA.
AC A3N3H7;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Protease 3 {ECO:0000256|ARBA:ARBA00017565};
DE EC=3.4.24.55 {ECO:0000256|ARBA:ARBA00012449};
DE AltName: Full=Pitrilysin {ECO:0000256|ARBA:ARBA00033450};
DE AltName: Full=Protease III {ECO:0000256|ARBA:ARBA00031184};
DE AltName: Full=Protease pi {ECO:0000256|ARBA:ARBA00029597};
GN Name=ptrA {ECO:0000313|EMBL:ABN74963.1};
GN OrderedLocusNames=APL_1883 {ECO:0000313|EMBL:ABN74963.1};
OS Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=416269 {ECO:0000313|EMBL:ABN74963.1, ECO:0000313|Proteomes:UP000001432};
RN [1] {ECO:0000313|EMBL:ABN74963.1, ECO:0000313|Proteomes:UP000001432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L20 {ECO:0000313|EMBL:ABN74963.1,
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 -!- FUNCTION: Endopeptidase that degrades small peptides of less than 7
CC kDa, such as glucagon and insulin. {ECO:0000256|ARBA:ARBA00002184}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; CP000569; ABN74963.1; -; Genomic_DNA.
DR AlphaFoldDB; A3N3H7; -.
DR STRING; 416269.APL_1883; -.
DR MEROPS; M16.001; -.
DR EnsemblBacteria; ABN74963; ABN74963; APL_1883.
DR KEGG; apl:APL_1883; -.
DR eggNOG; COG1025; Bacteria.
DR HOGENOM; CLU_004639_1_3_6; -.
DR Proteomes; UP000001432; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR032632; Peptidase_M16_M.
DR PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR Pfam; PF16187; Peptidase_M16_M; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABN74963.1};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:ABN74963.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001432};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..982
FT /note="Protease 3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002655556"
FT DOMAIN 74..200
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 235..416
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 420..696
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 704..880
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 982 AA; 109655 MW; 16E3CA19B6C44853 CRC64;
MISRAISYAL SATFALGIAL PTFANNPQNQ TASGEQKMLP IKAAGFEVLV QTINKSPNDK
AIYQAIRLQN GMTVLLISDE KANKSLMSLA LPIGSMEDPQ QQQGLAHYLE HMILMGSKQF
PETNSLDQFL TKNGGYNNAS TTSDRTAYYL EVNNNAFDEA VARLADAFAQ PLLSESNAKK
EVNAVNAEMV RAKSSDGHLL HSVNLATANP AHPITKFAVG NNQTLSDKEN SKLQAELEQF
YQRYYSSNLV KAVLYSNQSV EQLAALAERT LGKMQNKNLN VPTVDMPFFR TEDKGVLIEY
KPVQPTKLLS VSFDMPNDED KFAHKTGEYL AYVFSNNTEG TLSDYLIKQG LSDSGIAAVP
SANVSRNRGD FTFYVALTDK GLSEQDKVIS LIFQQIEQVK KDGIQESYFN EVRESLKQDF
QYLQVEKNGN YIEALAEQML HYPVEHILDS AYVVGAMDSE AIKAKLAAMT LDNARILVVS
EQAKTDKKTP YFEAGYSVRK FSDVEKTQWL DFSHNPSLKL PELNPYFATD FSLIKPSDER
KVPKALVSNE GKAIYAMPSQ YFAQDPKTIV SVSLSIMPKS DDLTETVSAT LLGYMNNLAQ
TKLAFQTAVA GMQAGVTPYP NGISIEAAGY TQHLAKLIGD TLTQFKTFEL SEAVLAQAKQ
RAFEALDGLS KASSLAQANA AISNFAAYPY FEEDKQRKAL NEMTLSDVKS IRDKLLEKST
GVSILSVGNL TDKQVENLAS EINAIVKNRE TERGRGRYLD LNDSTRKLNY IKNVPHEDNA
LSITYLAKGY DELAGSARAN LLRDIIGRWY FDDLRTEKQL GYVVSATNTK LGKTAGMRFM
VQSPNTTPAG IMQHNQRFFA ESLTKLTALS EQEFVKYRDS LIEKLQRKPE SLNQEFSQFT
FDFNRRNDLF NQRAKMIEAV RQLTRQDIVD FYKHTVIEQQ GFSFISQALG TKTKAEDAVK
PAGYEKVESI EQIQKQFPVK YY
//
