ID A0A0U5L2R7_9GAMM Unreviewed; 962 AA.
AC A0A0U5L2R7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=ptr {ECO:0000313|EMBL:CUU25082.1};
GN ORFNames=EM595_2851 {ECO:0000313|EMBL:CUU25082.1};
OS Duffyella gerundensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Duffyella.
OX NCBI_TaxID=1619313 {ECO:0000313|EMBL:CUU25082.1, ECO:0000313|Proteomes:UP000059419};
RN [1] {ECO:0000313|Proteomes:UP000059419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Blom J.;
RL Submitted (NOV-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}.
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DR EMBL; LN907827; CUU25082.1; -; Genomic_DNA.
DR RefSeq; WP_067433326.1; NZ_LN907827.1.
DR AlphaFoldDB; A0A0U5L2R7; -.
DR STRING; 1619313.EM595_2851; -.
DR KEGG; ege:EM595_2851; -.
DR PATRIC; fig|1619313.3.peg.2959; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000059419; Chromosome 1.
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:CUU25082.1};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:CUU25082.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000059419};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..962
FT /note="Protease 3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006861027"
FT DOMAIN 55..191
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 215..394
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 400..674
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 683..856
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 962 AA; 108245 MW; 6A709AAF918AB873 CRC64;
MRKNAVWIIS LLCCSLVAIS ARAADGWQPI NETINKSDKD TRQYQAIRLD NGMTVMLVSD
VQAPKSLAAL TLPIGSLDDP DSQLGLAHFL EHMVLMGSAR YPQPDNLAEF LKMHGGSHNA
STASYRTAFY LEVENDALAP AVDRLADAIA APRLDPINVE RERNAVNAEL TMARARDGLR
MQQVGAETLN PAHPGSRFSG GNLDTLRDKP DSKLLDTLKQ FYQQHYSANL MKAVIYSNRP
LPEMAHIAAD TFGRVPNRQA SVPAISVPAA TDAQQGIIIH YVPAQPRKQL KIEFRIDNNS
DKFRTKSDTL IAYLLGNRSR DTLSDWLQKQ GLADAINAGA DPVIDRNGGL FAISVNLTDK
GMLERDKVVA AVFSYINLLR QQGVDKRYFD EVAKVLNIDF RYPSITRDMG YIEWLVDLML
RVPVAHTLDA PYLADRYDAE AINARLAMMT PQHARIWYIG EKEPHNKVAY FVDAPYQVDK
ISSEKFAQWQ KMSDDMHLAM PTLNPYIPDD FSLIPPLEKA YIHPQELVNQ PGLRVFYMPS
RYFASEPKAN ITLALRNKAA MRDARSQVLF GLNDYLAGLA LDELNSQANV AGISFSSSED
DGIMFNASGF TQHLPALMQQ MLHGYISYQP DEAQFAQAKS FYLQQLDAAD RGKAFEQAIQ
PAQMLSRLPY TQRSERREVI KTLTLDDLQH YRQQLIQQAT PEMMVIGNMR ADSVTALATE
LKKQLGCQGD GWWHSEHIAF DKPIKANLQQ PGSSTDSALA ALYAPLGYNE YQGIAHSSMI
SQIIQPWFYN QLRTEEQLGY AVFAFQMPIG RQWGIGFLLQ SNVKQPAYLL QRYQAFYPQA
EKRLRDMQQK DFAQYQLAMI NDLQQRPQTL DEEAGRYSKD FDRENYQFDT REKAVEQIKQ
VTPASLADFF HQAVIAQNGL TMMSQVSGSH QGAADYAILP DYHTWAALSD LQQSMPVKSA
LQ
//
