ID   PTRA_SALTY              Reviewed;         962 AA.
AC   Q8ZMB5;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 113.
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=STM2995;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(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; AE006468; AAL21871.1; -; Genomic_DNA.
DR   RefSeq; NP_461912.1; NC_003197.2.
DR   RefSeq; WP_001138254.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZMB5; -.
DR   SMR; Q8ZMB5; -.
DR   STRING; 99287.STM2995; -.
DR   MEROPS; M16.001; -.
DR   PaxDb; Q8ZMB5; -.
DR   EnsemblBacteria; AAL21871; AAL21871; STM2995.
DR   GeneID; 1254518; -.
DR   KEGG; stm:STM2995; -.
DR   PATRIC; fig|99287.12.peg.3169; -.
DR   HOGENOM; CLU_004639_1_3_6; -.
DR   OMA; WIFDEMK; -.
DR   PhylomeDB; Q8ZMB5; -.
DR   BioCyc; SENT99287:STM2995-MON; -.
DR   Proteomes; UP000001014; 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; IBA:GO_Central.
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_0000026762"
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;  107486 MW;  322AD6E87B873952 CRC64;
     MPRSTWFKAL LLLVALWGPA VQADIGWQPL QETIRKSDKD TRQYQAIRLD NDMVVLLVSD
     PQAVKSLSAL VVPVGSLEDP 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 AIFSYLNMLR EKGIDKRYFD ELAHVLDLDF RYPSITRDMD YVEWLADTMI
     RVPVAHTLDA ANIADRYDPA AIKNRLAMMT PQNARIWYIS PQEPHNKTAY FVDAPYQVDK
     ISEQTFKNWQ QKAQGIALSL PELNPYIPDD FTLVKNDKNY 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