ID   PTRA_ECOL6              Reviewed;         962 AA.
AC   Q8CVS2;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=c3415;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014075; AAN81860.1; -; Genomic_DNA.
DR   RefSeq; WP_001138109.1; NC_004431.1.
DR   AlphaFoldDB; Q8CVS2; -.
DR   SMR; Q8CVS2; -.
DR   STRING; 199310.c3415; -.
DR   MEROPS; M16.001; -.
DR   EnsemblBacteria; AAN81860; AAN81860; c3415.
DR   KEGG; ecc:c3415; -.
DR   eggNOG; COG1025; Bacteria.
DR   HOGENOM; CLU_004639_1_3_6; -.
DR   OMA; WIFDEMK; -.
DR   BioCyc; ECOL199310:C3415-MON; -.
DR   Proteomes; UP000001410; 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   Signal; Zinc.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..962
FT                   /note="Protease 3"
FT                   /id="PRO_0000026760"
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;  107892 MW;  DEDD2CA2A9AADF8D CRC64;
     MPRSIWFKAL LLFVALWAPL 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 KKAANIALSL PELNPYIPDD FSLIKSEKKY DHPELIVDES NLRVVYAPSR
     YFASEPKADV SLILRNPKAM DSARNQVMFA LNDYLAGLAL DQLSNQASVG GISFSTNANN
     GLMVNANGYT QRLPQLFQAL LEGYFSYTAT EDQLEQAKSW YNQMMDSAEK GKAFEQAIMP
     AQMLSQVPYF SRDERRKILP SITLKEVLAY RDALKSGARP EFMVIGNMTE AQATTLARHV
     QKQLGADGSE WCRNKDVVVD KKQSVIFEKA GNSTDSALAA IFVPTGYDEY TSSAYSSLLG
     QIVQPWFYNQ LRTEEQLGYA VFAFPMSVGR QWGMGFLLQS NDKQPSFLWE RYKAFFPTAE
     AKLRTMKPEE FAQIQQAVIT QMLQAPQTLG EEASKLSKDF DRGNMRFDSR DKIVAQIKLL
     TPQKLADFFH QAVVEPQGMA ILSQISGSQN GKAEYVHPEG WKVWENVSAL QQTMPLMSEK
     NE