ID C5S3U4_9PAST Unreviewed; 985 AA.
AC C5S3U4;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 70.
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 ORFNames=AM305_01719 {ECO:0000313|EMBL:EER46434.1};
OS Actinobacillus minor NM305.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=637911 {ECO:0000313|EMBL:EER46434.1, ECO:0000313|Proteomes:UP000005532};
RN [1] {ECO:0000313|EMBL:EER46434.1, ECO:0000313|Proteomes:UP000005532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM305 {ECO:0000313|EMBL:EER46434.1,
RC ECO:0000313|Proteomes:UP000005532};
RX PubMed=19819087; DOI=10.1016/j.vetmic.2009.09.030;
RA Arya G., Niven D.F.;
RT "Production of haemolysins by strains of the Actinobacillus
RT minor/"porcitonsillarum" complex.";
RL Vet. Microbiol. 141:332-341(2010).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EER46434.1}.
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DR EMBL; ACQL01000112; EER46434.1; -; Genomic_DNA.
DR RefSeq; WP_005825184.1; NZ_ACQL01000112.1.
DR AlphaFoldDB; C5S3U4; -.
DR MEROPS; M16.001; -.
DR eggNOG; COG1025; Bacteria.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000005532; Unassembled WGS sequence.
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};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:EER46434.1};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..985
FT /note="Protease 3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002957111"
FT DOMAIN 77..211
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 238..419
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 423..697
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 705..883
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 985 AA; 112113 MW; F11A6C501FCEE57E CRC64;
MKKTLINRSI RYAIYTFLLA TQITPATLAK NMENPTANVT EIAGSSLGFE LIKTTINKSP
NDKALYQAIT LKNGMTVLLI SDEKANKSLM SAAIPVGSME DPITQQGLAH YLEHMILMGS
KHYPETNSFD KFLNENGGYN NASTAPYRTA YYFEVNNNAF DEAVARFADT LAFPLLSESN
AKKEVNAVNA EMVRAKSNDG YLLHSVNLAT ANPAHPMTKF AVGNNETLSD KPNSKLQDEL
IAFYQKYYSA NLFKAVLYSN QSIEQLAKLA EKTLGKMENK QLKKPKVNVP LFRNEDKGVI
IHYNPLQPEK LLSISFDMPN DEDKFKYKTG EYLAYIFSNN TEGTLSDYLI KQGLSDSGIE
AQSDPNFSRN RGEFTFYVAL TEKGLKEKDK IISLIFQQIE KVKKEGIKEN YFNELRESLK
QEFTHLQVEK DSTYIETLVE KMLFYPTEHL LDESYLAEQM DTKAIEEKLS AMTLDNARIL
LVEENAKTDK FSPYYRAGYA IEKITEAQKK QWLDFSQNPS INLPALNPYF ATDFSLIKKE
QREVPELVAQ AQGERIYAMA SQYFSEDPKA RIALNFSIMP RTDDLKESIS ATILSYMNNL
AQTQLNFQAS VAGINTEINT SANGMTLQTE GYTQHLPKLI VDYLTRFSQF ELNEKFLAQA
KQRLIEALDG KKTANSLNQA NEIFANFASY PYFEEDKQRK MIAEITLADI QKIREKLLSQ
ATGLKVLSVG NLSDQQVKDL SKEVTKVIQN KNTALAKYRY LDINQSSRKL NVVKNVPNED
NALSIAFMAK DYAEMDSYVR ALFLKDMISR WYFDDLRTNK QLGYVVYATN GRIGTTSGLR
FMVQSPNTSP KGIMEHNQRF FAESLEKLTA LSEAEFNQFK ESLLNKLTRK PESLSQEFSL
FTYDFSLLNN RFDYRQKTIE AVKQLTKQDI VKFYQDTVID QKGLVLVSQA LGTKTKSTDT
AVLSGFENIE NIENLQKEFQ LKFYE
//
