PTRA_ECO57
ID PTRA_ECO57 Reviewed; 962 AA.
AC Q8X6M8;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protease 3;
DE EC=3.4.24.55;
DE AltName: Full=Pitrilysin;
DE AltName: Full=Protease III;
DE AltName: Full=Protease pi;
DE Flags: Precursor;
GN Name=ptrA; Synonyms=ptr; OrderedLocusNames=Z4138, ECs3678;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Endopeptidase that degrades small peptides of less than 7
CC kDa, such as glucagon and insulin. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage of 16-Tyr-|-Leu-17 and 25-Phe-|-Tyr-26
CC bonds of oxidized insulin B chain. Also acts on other substrates of
CC Mw less than 7 kDa such as insulin and glucagon.; EC=3.4.24.55;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10096};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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DR EMBL; AE005174; AAG57932.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37101.1; -; Genomic_DNA.
DR PIR; F91088; F91088.
DR PIR; H85933; H85933.
DR RefSeq; NP_311705.1; NC_002695.1.
DR RefSeq; WP_001138211.1; NZ_SEKU01000002.1.
DR AlphaFoldDB; Q8X6M8; -.
DR SMR; Q8X6M8; -.
DR STRING; 155864.EDL933_3999; -.
DR MEROPS; M16.001; -.
DR EnsemblBacteria; AAG57932; AAG57932; Z4138.
DR EnsemblBacteria; BAB37101; BAB37101; ECs_3678.
DR GeneID; 916510; -.
DR KEGG; ece:Z4138; -.
DR KEGG; ecs:ECs_3678; -.
DR PATRIC; fig|386585.9.peg.3845; -.
DR eggNOG; COG1025; Bacteria.
DR HOGENOM; CLU_004639_1_3_6; -.
DR OMA; WIFDEMK; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR Pfam; PF16187; Peptidase_M16_M; 1.
DR SUPFAM; SSF63411; SSF63411; 4.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Metalloprotease; Periplasm; Protease;
KW Reference proteome; Signal; Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..962
FT /note="Protease 3"
FT /id="PRO_0000026759"
FT ACT_SITE 91
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
SQ SEQUENCE 962 AA; 107808 MW; 30785644CBF0E452 CRC64;
MPRSTWFKAL LLLVALWAPL SQAETGWQPI QETIRKSDKD NRQYQAIRLD NGMVVLLVSD
PQAVKSLSAL VVPVGSLEDP EAYQGLAHYL EHMSLMGSKK YPQADSLAEY LKMHGGSHNA
STAPYRTAFY LEVENDALPG AVDRLADAIA EPLLDKKYAE RERNAVNAEL TMARTRDGMR
MAQVSAETIN PAHPGSKFSG GNLETLSDKP GNPVQQALKD FHEKYYSANL MKAVIYSNKP
LPELAKMAAD TFGRVPNKES KKPEITVPVV TDAQKGIIIH YVPALPRKVL RVEFRIDNNS
AKFRSKTDEL ITYLIGNRSP GTLSDWLQKQ GLVEGISANS DPIVNGNSGV LAISASLTDK
GLANRDQVVA AIFSYLNLLR EKGIDKQYFD ELANVLDIDF RYPSITRDMD YVEWLADTMI
RVPVEHTLDA VNIADRYDAK AVKERLAMMT PQNARIWYIS PKEPHNKTAY FVDAPYQVDK
ISEQTFADWQ QKAANIALSL PELNPYIPDD FSLIKSEKKY DHPELIVDES NLRVVYAPSR
YFSSEPKADV SLILRNPKAM DSARNQVMFA LNDYLAGLAL DQLSNQASVG GISFSTNANN
GLMVNANGYT QRLPQLFQAL LEGYFSYTAT EDQLEQAKSW YNQMMDSAEK GKAFEQAIMP
AQMLSQVPYF SRDERRKILP SITLKEVLAY RDALKSGARP EFMVIGNMTE AQATTLARDV
QKQLGADGSE WCRNKDVVVD KKQSVIFEKA GNSTDSALAA VFVPTGYDEY TSSAYSSLLG
QIVQPWFYNQ LRTEEQLGYA VFAFPMSVGR QWGMGFLLQS NDKQPSFLWE RYKAFFPTAE
AKLRAMKPDE FAQIQQAVIT QMLQAPQTLG EEALKLSKDF DRGNMRFDSR DKIVAQIKLL
TPQKLADFFH QAVVEPQGMA ILSQISGSQN GKAEYVHPEG WKVWENVSAL QQTMPLMSEK
NE
