ID   PTRB_ECOLI              Reviewed;         686 AA.
AC   P24555; P78068;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=Protease 2;
DE            EC=3.4.21.83;
DE   AltName: Full=Oligopeptidase B;
DE   AltName: Full=Protease II;
GN   Name=ptrB; Synonyms=tlp; OrderedLocusNames=b1845, JW1834;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 33694 / HB101;
RX   PubMed=1769955; DOI=10.1093/oxfordjournals.jbchem.a123577;
RA   Kanatani A., Masuda T., Shimoda T., Misoka F., Lin X.S., Yoshimoto T.,
RA   Tsuru D.;
RT   "Protease II from Escherichia coli: sequencing and expression of the enzyme
RT   gene and characterization of the expressed enzyme.";
RL   J. Biochem. 110:315-320(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA   Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA   Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA   Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA   Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA   Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA   Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 40.1-50.0 min region on the linkage map.";
RL   DNA Res. 3:379-392(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
CC   -!- FUNCTION: Cleaves peptide bonds on the C-terminal side of lysyl and
CC       argininyl residues.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of -Arg-|-Xaa- and -Lys-|-Xaa- bonds in
CC         oligopeptides, even when P1' residue is proline.; EC=3.4.21.83;
CC   -!- SIMILARITY: Belongs to the peptidase S9A family. {ECO:0000305}.
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DR   EMBL; D10976; BAA01750.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74915.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15651.1; -; Genomic_DNA.
DR   PIR; E64946; E64946.
DR   RefSeq; NP_416359.1; NC_000913.3.
DR   RefSeq; WP_000936927.1; NZ_LN832404.1.
DR   AlphaFoldDB; P24555; -.
DR   SMR; P24555; -.
DR   BioGRID; 4263144; 21.
DR   IntAct; P24555; 3.
DR   STRING; 511145.b1845; -.
DR   ESTHER; ecoli-ptrb; S9N_PREPL_Peptidase_S9.
DR   MEROPS; S09.010; -.
DR   jPOST; P24555; -.
DR   PaxDb; 511145-b1845; -.
DR   EnsemblBacteria; AAC74915; AAC74915; b1845.
DR   GeneID; 946358; -.
DR   KEGG; ecj:JW1834; -.
DR   KEGG; eco:b1845; -.
DR   PATRIC; fig|1411691.4.peg.405; -.
DR   EchoBASE; EB0997; -.
DR   eggNOG; COG1770; Bacteria.
DR   HOGENOM; CLU_011290_0_1_6; -.
DR   InParanoid; P24555; -.
DR   OMA; LDPWFSH; -.
DR   OrthoDB; 9801421at2; -.
DR   PhylomeDB; P24555; -.
DR   BioCyc; EcoCyc:EG11004-MONOMER; -.
DR   BioCyc; MetaCyc:EG11004-MONOMER; -.
DR   BRENDA; 3.4.21.83; 2026.
DR   PRO; PR:P24555; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR   GO; GO:0070012; F:oligopeptidase activity; IDA:EcoCyc.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:EcoCyc.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002471; Pept_S9_AS.
DR   InterPro; IPR023302; Pept_S9A_N.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002470; Peptidase_S9A.
DR   PANTHER; PTHR11757:SF19; PROLYL ENDOPEPTIDASE-LIKE; 1.
DR   PANTHER; PTHR11757; PROTEASE FAMILY S9A OLIGOPEPTIDASE; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   Pfam; PF02897; Peptidase_S9_N; 1.
DR   PRINTS; PR00862; PROLIGOPTASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Protease; Reference proteome;
KW   Serine protease.
FT   CHAIN           1..686
FT                   /note="Protease 2"
FT                   /id="PRO_0000122404"
FT   ACT_SITE        532
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084,
FT                   ECO:0000269|PubMed:1769955"
FT   ACT_SITE        617
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        652
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   CONFLICT        682..686
FT                   /note="ATPAD -> LRLRTKYFPDNVSVLNAAPGSCCPGY (in Ref. 1; AA
FT                   sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   686 AA;  79491 MW;  B41AD388044D56B2 CRC64;
     MLPKAARIPH AMTLHGDTRI DNYYWLRDDT RSQPEVLDYL QQENSYGHRV MASQQALQDR
     ILKEIIDRIP QREVSAPYIK NGYRYRHIYE PGCEYAIYQR QSAFSEEWDE WETLLDANKR
     AAHSEFYSMG GMAITPDNTI MALAEDFLSR RQYGIRFRNL ETGNWYPELL DNVEPSFVWA
     NDSWIFYYVR KHPVTLLPYQ VWRHAIGTPA SQDKLIYEEK DDTYYVSLHK TTSKHYVVIH
     LASATTSEVR LLDAEMADAE PFVFLPRRKD HEYSLDHYQH RFYLRSNRHG KNFGLYRTRM
     RDEQQWEELI PPRENIMLEG FTLFTDWLVV EERQRGLTSL RQINRKTREV IGIAFDDPAY
     VTWIAYNPEP ETARLRYGYS SMTTPDTLFE LDMDTGERRV LKQTEVPGFY AANYRSEHLW
     IVARDGVEVP VSLVYHRKHF RKGHNPLLVY GYGSYGASID ADFSFSRLSL LDRGFVYAIV
     HVRGGGELGQ QWYEDGKFLK KKNTFNDYLD ACDALLKLGY GSPSLCYAMG GSAGGMLMGV
     AINQRPELFH GVIAQVPFVD VVTTMLDESI PLTTGEFEEW GNPQDPQYYE YMKSYSPYDN
     VTAQAYPHLL VTTGLHDSQV QYWEPAKWVA KLRELKTDDH LLLLCTDMDS GHGGKSGRFK
     SYEGVAMEYA FLVALAQGTL PATPAD
//