ID   PTRA_SALTI              Reviewed;         962 AA.
AC   Q8Z418;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 118.
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=STY3133, t2903;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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   -!- 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; AL513382; CAD02819.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO70457.1; -; Genomic_DNA.
DR   RefSeq; NP_457388.1; NC_003198.1.
DR   RefSeq; WP_001138262.1; NZ_WSUR01000005.1.
DR   AlphaFoldDB; Q8Z418; -.
DR   SMR; Q8Z418; -.
DR   STRING; 220341.16504073; -.
DR   MEROPS; M16.001; -.
DR   EnsemblBacteria; AAO70457; AAO70457; t2903.
DR   KEGG; stt:t2903; -.
DR   KEGG; sty:STY3133; -.
DR   PATRIC; fig|220341.7.peg.3188; -.
DR   eggNOG; COG1025; Bacteria.
DR   HOGENOM; CLU_004639_1_3_6; -.
DR   OMA; WIFDEMK; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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; 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.
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_0000026761"
FT   ACT_SITE        91
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   962 AA;  107524 MW;  5745C2C77F7F5832 CRC64;
     MPRSTWFKAL LLLVALWGPA VQADIGWQPL QETIRKSDKD TRQYQAIRLD NDMVVLLVSD
     PQAVKSLSAL VVPVVSLEDP EAHQGLAHYL EHMCLMGSKK YPQADSLAEY LKRHGGSHNA
     STAPYRTAFY LEVENDALPG AVDRLADAIA APLLNKKYAE RERNAVNAEL TMARTRDGMR
     MAQVSAETIN PAHPGSHFSG GNLETLSDKP GNPVQQALIA FHEKYYSSNL MKAVIYSNKP
     LPELASIAAA TYGRVPNKQI KKPEITVPVI TEAQKGIIIH YVPALPRKVL RVEFRIDNNS
     AQFRSKTDEL VSYLIGNRSP GTLSDWLQKQ GLVEGISADS DPIVNGNSGV FAISATLTDK
     GLANRDEVVA AIFSYLNTLR EKGIDKRYFD ELAHVLDLDF RYPSITRDMD YVEWLADTMI
     RVPVAHTLDA ANIADRYDPA AIKNRLAMMT PQNARIWYIS PQEPHNKIAY FVDAPYQVDK
     ISEQTFKNWQ QKAQGIALSL PELNPYIPDD FTLIKNDKNY VRPELIVDKA DLRVVYAPSR
     YFASEPKADV SVVLRNPQAM DSARNQVLFA LNDYLAGMAL DQLSNQAAVG GISFSTNANN
     GLMVTANGYT QRLPQLFLAL LEGYFSYDAT EEQLAQAKSW YTQMMDSAEK GKAYEQAIMP
     VQMISQVPYF SRDERRALLP SITLKEVMAY RNALKTGARP EFLVIGNMSE AQATSLAQDV
     QKQLAANGSA WCRNKDVVVE KKQSVIFEKA GSSTDSALAA VFVPVGYDEY VSAAYSAMLG
     QIVQPWFYNQ LRTEEQLGYA VFAFPMSVGR QWGMGFLLQS NDKQPSYLWQ RYQAFFPDAE
     AKLRAMKPEE FAQIQQAIIT QMRQAPQTLG EEASRLSKDF DRGNMRFDSR DKIIAQIKLL
     TPQKLADFFH QAVVEPQGMA ILSQIAGSQN GKAEYVHPTG WKVWDNVSAL QQTLPLMSEK
     NE