PTRB_ECOLI
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 03-AUG-2022, entry version 159.
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; Proteobacteria; 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; P24555; -.
DR PRIDE; P24555; -.
DR EnsemblBacteria; AAC74915; AAC74915; b1845.
DR EnsemblBacteria; BAA15651; BAA15651; BAA15651.
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; NMGAGHG; -.
DR PhylomeDB; P24555; -.
DR BioCyc; EcoCyc:EG11004-MON; -.
DR BioCyc; MetaCyc:EG11004-MON; -.
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; -; 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 Pfam; PF00326; Peptidase_S9; 1.
DR Pfam; PF02897; Peptidase_S9_N; 1.
DR PRINTS; PR00862; PROLIGOPTASE.
DR SUPFAM; SSF53474; SSF53474; 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
