ID Q6D8I0_PECAS Unreviewed; 982 AA.
AC Q6D8I0;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 103.
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:CAG73905.1};
GN Synonyms=ptr {ECO:0000313|EMBL:CAG73905.1};
GN OrderedLocusNames=ECA0994 {ECO:0000313|EMBL:CAG73905.1};
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491 {ECO:0000313|EMBL:CAG73905.1, ECO:0000313|Proteomes:UP000007966};
RN [1] {ECO:0000313|EMBL:CAG73905.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SCRI1043 {ECO:0000313|EMBL:CAG73905.1};
RA Bell K.S., Sebaihia M., Pritchard L., Holden M., Hyman L.J., Holeva M.C.,
RA Thomson N.R., Bentley S.D., Churcher C., Mungall K., Atkin R., Bason N.,
RA Brooks K., Chillingworth T., Clark K., Doggett J., Fraser A., Hance Z.,
RA Hauser H., Jagels K., Moule S., Norbertczak H., Ormond D., Price C.,
RA Quail M.A., Sanders M., Walker D., Whitehead S., Salmond G.P.C.,
RA Birch P.R.J., Barrell B.G., Parkhill J., Toth I.K.;
RT "The genome sequence of the enterobacterial phytopathogen Erwinia
RT carotovora subsp. atroseptica SCRI1043 and functional genomic
RT identification of novel virulence factors.";
RL Submitted (FEB-2004) 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; BX950851; CAG73905.1; -; Genomic_DNA.
DR RefSeq; WP_011092594.1; NC_004547.2.
DR AlphaFoldDB; Q6D8I0; -.
DR STRING; 218491.ECA0994; -.
DR MEROPS; M16.001; -.
DR GeneID; 57207821; -.
DR KEGG; eca:ECA0994; -.
DR PATRIC; fig|218491.5.peg.1000; -.
DR eggNOG; COG1025; Bacteria.
DR HOGENOM; CLU_004639_1_3_6; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000007966; 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:CAG73905.1};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:CAG73905.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007966};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
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 683..858
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 955..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 982 AA; 110172 MW; 3E601359494C91D3 CRC64;
MRKQWVWITG WFLLFTFWLP ASWAETGWQP LAQTIRKSEK DPRQYQAIKL DNGMTVLLVS
DPQAPKSLAS LALPIGSLDD PNNQLGLAHY LEHMVLMGSK RYPEPEALSE FLKKHGGSHN
ASTASYRTAF YLEVENDALR PAVDRMADAI AEPLLDPVNA DRERNAVNAE LTMARSRDGH
RMAQVGAETL NPAHPSARFS GGNLETLSDK PGSKLHDELV KFYQQYYSAN LMKGVIYSNQ
PLPELAKLAV DTFGRIANHN ASIPAVTVPV TTEKQRGVMI HYVPAQPRKQ LRIEFRVSDI
SQEFRSKTDT YISYLLGNRS QNTLSDWLQK EGLVESIGAG SSPIIDRNGG MFAISASLTD
KGLAQRDEVI AAIFRYLQQI RTEGIQQRYF DEIAHVMDLD FRYPSISRDM DYIEWLVDTM
LRVPVEHTLD AQYVADRYDP KAIAARLDEM TPQNARVWVI SPNEPHNKVA YFVDAPYEMD
KIPSATFAKW KTLGQKMSLS LPTINPYIPD DFSLINADKA ITKPTLLLNQ PGLRVLYMPS
HYFADEPKAE ITLFLRNQEV RSTARNQVLF ALNDYLAGLA LDELSYQASI GGISFSTRSN
DGLVISADGY TQHLPRLLLT LADGYASFTS TEAQLEQAKS WYLQQLDAVE KSKAFEQALQ
PIQAVSQLPY FERGERRKLL KDIRLQDVVN YRNDLLQKAT PEMLVVGNLA PERVTELANT
LKAHLKANGE NLSRSDDVKV SKPQLANLQR PGSSTDSALA AVYVPTGYSE TQSMAYGSVL
GQIVQPWFYS QLRTEEQLGY AVFAFPTTVG RQMGIGFLLQ SNSKQPAYLY QRYEDFFLKA
QKRLREMSED EFAQYKQGVM NELSQRPQTL GEEASRLRSD LDRENFAFDS REKLLEQIKP
LTVKQLADFF QQALKPEGLA VLSQVSGSHH GKADYAAPKG WHTYADASSL QKTLPREKAP
TMIPAPAAQP AASEAVGKVS AE
//
