ID A0A0M2KEK8_9GAMM Unreviewed; 962 AA.
AC A0A0M2KEK8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SY86_08200 {ECO:0000313|EMBL:KKF35406.1};
OS Erwinia tracheiphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=65700 {ECO:0000313|EMBL:KKF35406.1, ECO:0000313|Proteomes:UP000033924};
RN [1] {ECO:0000313|EMBL:KKF35406.1, ECO:0000313|Proteomes:UP000033924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BuffGH {ECO:0000313|EMBL:KKF35406.1,
RC ECO:0000313|Proteomes:UP000033924};
RA Shapiro L.R.;
RT "Erwinia tracheiphila.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KKF35406.1}.
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DR EMBL; JXNU01000003; KKF35406.1; -; Genomic_DNA.
DR RefSeq; WP_016190206.1; NZ_JXNU01000003.1.
DR AlphaFoldDB; A0A0M2KEK8; -.
DR STRING; 65700.SY86_08200; -.
DR PATRIC; fig|65700.7.peg.2071; -.
DR Proteomes; UP000033924; 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:KKF35406.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033924};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..962
FT /note="Protease 3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005636085"
FT DOMAIN 56..192
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 216..394
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 401..672
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 682..858
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 962 AA; 108060 MW; EE7DCA07DAE58C55 CRC64;
MRYFAAWFTA LILLATGWSQ LVQAQSGWQV LPDTVRKSDR DPRQYQAVRL DNGMTVLLVS
DPLASKSLAA LAIPVGSLEN PRNQQGLAHY LEHMLLMGSE HYPEPDNLAE FLKKHGGIHN
ASTASYRTAF YLEVENDALQ PAVDRLADAI AAPRLAPVNA DRERHAVNAE LTMARSRDGL
RMVQVGAETL NPQHPASLFS GGNLETLKDK PDSNLHDALK AFYHRYYSAN LMKAVIYSNK
PLEALQKIAV TTFGRVENRN ATVPEITVPV VTDKQKGIII HYVPAQPHRQ LRIEFRIDNN
SDQFRSKTDT LIAYMIGNRS KNTLSDWLQN NGLADSIDAG ADPLVDRNGG VFSISVSLTD
KGLTERDRVI AAVFSYLNCL RTGGIDKRYF DEMAHVLDLD FRYPSITRDM DYIQWLVDTM
LRVPVTDTLD AGYIADKFDP QAIQARLDEM TPRNARFWFI GPNEPHNKMA YFVNAPYQVD
TISAQRFADW QAESNKISLS LPVLNPWIPD DFTLIAPQHQ YDHPQALVSE PGLKVFYMPS
QFYADDPRAN ITLYLRNQAA RSTAKNQVLF SLNDYLAGLA LDELSSQASV GGIGFSTSQN
DGVAFNVSGF TQHLPELMKA LLKEYAHFQA TEAQLEQARS WYLERLDSAE KGKAFEEAIQ
PARLLSQIPY TQRDERRRLL KSITLQDLNA YRQMLLQNAT PELLVVGNMT KESSKTLASD
IKTQLGCQGE SGWRSSYPDV DKKTFANMQK AGSSTDSALA ALYVPAGYDE YASIASAALL
SQIVQPWFYN QLRTEEQLGY AVFAFQMSVG RQWGIAFVLQ SNVKQPAYLL RRFDAFYPTA
EQRLRAISKE DFAQYQAAMI NELRQRPQTL DEEAGRFAKD FTRENYRFDS RAKVIHQIEA
LSPEKLAAFF HDAVIAPRGL VLLSQISGSQ HGKEDYAVPA GFTTWQDVSS LQQSLPVKSD
KP
//
