ID A0A0J8YI15_9GAMM Unreviewed; 961 AA.
AC A0A0J8YI15;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=AI28_11940 {ECO:0000313|EMBL:KMV69045.1};
OS bacteria symbiont BFo1 of Frankliniella occidentalis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae.
OX NCBI_TaxID=1628855 {ECO:0000313|EMBL:KMV69045.1, ECO:0000313|Proteomes:UP000037152};
RN [1] {ECO:0000313|EMBL:KMV69045.1, ECO:0000313|Proteomes:UP000037152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFo1 {ECO:0000313|EMBL:KMV69045.1,
RC ECO:0000313|Proteomes:UP000037152};
RA Facey P.D., Hitchings M.D., Hegarty M.J., Pachebat J.A., Morgan L.V.,
RA Hoeppner J.E., Whitten M.A., Dyson P.J., Del Sol R.;
RT "The draft genomes, genome evolution and classification of BFo1 and BFo2
RT two insect symbionts isolated from Western Flower Thrips (Frankliniella
RT occidentalis [Pergande]).";
RL Submitted (MAY-2014) 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:KMV69045.1}.
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DR EMBL; JMSO01000185; KMV69045.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8YI15; -.
DR STRING; 1628855.WB66_17275; -.
DR PATRIC; fig|1628855.3.peg.2410; -.
DR Proteomes; UP000037152; 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:KMV69045.1};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..961
FT /note="Protease 3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005312291"
FT DOMAIN 55..192
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 215..393
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 400..671
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 682..857
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 961 AA; 107704 MW; 4EF007FA06F44E3D CRC64;
MRRYAVWLAC FVSVTLFAPL VQAQDGWQPI TETIRKSEKD PRQYQAIKLD NGMTVLLVSD
AQATKSLAAL TLPVGSLENP TDQLGLAHYL EHMVLMGSKR YPQPDNLAEF LKKHGGSHNA
STASYRTAFY LEVENDALQP AVDRLADAIA EPLLDPVNAD RERHAVNAEL TMARSRDGLR
MAQVGAETLN PEHPSSRFSG GNLETLRDKP GSKLHDALTA FYHRYYSANL MKAVIYGNQP
LPELQKIAAA TFGRVANHHA TVPDISVPVV TDKQKGIIIH YVPAQPRKQL KIEFRIDNNS
DKFRSKTDTL IGYLIGNRSK NTLSDWLQNQ GLADSISAGA DPVIDRNGGV FSIAISLTDQ
GQAKRDEVIA AVFSYLNQLR TEGIDKRYFD EVAHVLDLDF RYPSITRDMD YIEWLVDTML
RVPVADTLVA PYIADDYDAQ AIGARLDGMT PENARIWFIS PKEPHNKTAY FVDAPYQVDK
ISAQRFKDWQ VESDKIKLSL PVLNPYIPDD FSLIKADKAY ARPQELMNQQ GLRVFYMPSQ
YYADEPKANI TLALRNKAAM STAQNQVMFA LNDYLAGVAL DELSSQASVG GISFSTSEDD
GVTFSATGFT QRLPKLMSQL LKGYTSFTPT QAQLEQAKSW YLERLDAADK GKAFELAIQP
AQLLSQLPYT QRSERRKLVA TISLQQLMDY RKMLLEQSAP ELMVVGNMTP DAVRSLATEV
KTQLNCEGHE WWHSEHVTIT KPTLANLQEA GSSTDSALAA VYVPVGFEEY QSMASSAMLS
QIIQPWFYNQ LRTEEQLGYA VFAFQMPVGR QWGIGFLLQS NVKQPAFLLS RFKAFYPTAE
KRLREMSKAD FAQYQAAMIN ELKQRPQTLD EEAGRFSKDF DRENYKFDTR EKVIAQIQAL
TPQSVADFFH QAVMAPTGLA LLSQISGSHH GKADYAKEKG WTTWKDLSTL QQSLPVSQDT
P
//