PTRA_ECOLI
ID PTRA_ECOLI Reviewed; 962 AA.
AC P05458; P78106; Q2MA16;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 184.
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=b2821, JW2789;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3534791; DOI=10.1093/nar/14.19.7695;
RA Finch P.W., Wilson R.E., Brown K., Hickson I.D., Emmerson P.T.;
RT "Complete nucleotide sequence of the Escherichia coli ptr gene encoding
RT protease III.";
RL Nucleic Acids Res. 14:7695-7703(1986).
RN [2]
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 [3]
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 853-962.
RX PubMed=3537960; DOI=10.1093/nar/14.21.8573;
RA Finch P.W., Storey A., Chapman K.E., Brown K., Hickson I.D., Emmerson P.T.;
RT "Complete nucleotide sequence of the Escherichia coli recB gene.";
RL Nucleic Acids Res. 14:8573-8582(1986).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-296.
RC STRAIN=K12;
RX PubMed=3308636; DOI=10.1016/0378-1119(87)90486-0;
RA Claverie-Martin F., Diaz-Torres M.R., Kushner S.R.;
RT "Analysis of the regulatory region of the protease III (ptr) gene of
RT Escherichia coli K-12.";
RL Gene 54:185-195(1987).
RN [6]
RP MUTAGENESIS, AND ACTIVE SITE.
RX PubMed=1570301; DOI=10.1073/pnas.89.9.3835;
RA Becker A.B., Roth R.A.;
RT "An unusual active site identified in a family of zinc
RT metalloendopeptidases.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:3835-3839(1992).
RN [7]
RP MUTAGENESIS, AND ACTIVE SITE.
RX PubMed=8099278; DOI=10.1042/bj2920137;
RA Becker A.B., Roth R.A.;
RT "Identification of glutamate-169 as the third zinc-binding residue in
RT proteinase III, a member of the family of insulin-degrading enzymes.";
RL Biochem. J. 292:137-142(1993).
RN [8]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
CC -!- FUNCTION: Endopeptidase that degrades small peptides of less than 7
CC kDa, such as glucagon and insulin.
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;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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DR EMBL; X04581; CAA28249.1; -; Genomic_DNA.
DR EMBL; U29581; AAB40468.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75860.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76890.1; -; Genomic_DNA.
DR EMBL; X06227; CAA29576.1; -; Genomic_DNA.
DR EMBL; M17095; AAA24436.1; -; Genomic_DNA.
DR PIR; F65064; SNECPI.
DR RefSeq; NP_417298.1; NC_000913.3.
DR RefSeq; WP_001138201.1; NZ_LN832404.1.
DR PDB; 1Q2L; X-ray; 2.20 A; A=24-962.
DR PDBsum; 1Q2L; -.
DR AlphaFoldDB; P05458; -.
DR SMR; P05458; -.
DR BioGRID; 4262308; 35.
DR IntAct; P05458; 12.
DR STRING; 511145.b2821; -.
DR MEROPS; M16.001; -.
DR jPOST; P05458; -.
DR PaxDb; P05458; -.
DR PRIDE; P05458; -.
DR EnsemblBacteria; AAC75860; AAC75860; b2821.
DR EnsemblBacteria; BAE76890; BAE76890; BAE76890.
DR GeneID; 947284; -.
DR KEGG; ecj:JW2789; -.
DR KEGG; eco:b2821; -.
DR PATRIC; fig|1411691.4.peg.3915; -.
DR EchoBASE; EB0779; -.
DR eggNOG; COG1025; Bacteria.
DR HOGENOM; CLU_004639_1_3_6; -.
DR InParanoid; P05458; -.
DR OMA; WIFDEMK; -.
DR PhylomeDB; P05458; -.
DR BioCyc; EcoCyc:EG10786-MON; -.
DR BioCyc; MetaCyc:EG10786-MON; -.
DR EvolutionaryTrace; P05458; -.
DR PRO; PR:P05458; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:EcoliWiki.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
DR GO; GO:0006508; P:proteolysis; IDA:EcoliWiki.
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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Magnesium; Metal-binding; Metalloprotease;
KW Periplasm; Protease; Reference proteome; Signal; Zinc.
FT SIGNAL 1..23
FT CHAIN 24..962
FT /note="Protease 3"
FT /id="PRO_0000026758"
FT ACT_SITE 91
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096,
FT ECO:0000269|PubMed:1570301, ECO:0000269|PubMed:8099278"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096,
FT ECO:0000269|PubMed:1570301"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096,
FT ECO:0000269|PubMed:1570301"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT MUTAGEN 88
FT /note="H->R: Loss of activity and of Zn-binding."
FT MUTAGEN 91
FT /note="E->Q: Loss of activity."
FT MUTAGEN 92
FT /note="H->R: Loss of activity and of Zn-binding."
FT MUTAGEN 162
FT /note="E->Q: 20% loss of activity."
FT MUTAGEN 169
FT /note="E->Q: Loss of activity and of Zn-binding."
FT MUTAGEN 204
FT /note="E->Q: No loss of activity."
FT CONFLICT 277..284
FT /note="IIIHYVPA -> HYHSLRPW (in Ref. 5; AAA24436)"
FT /evidence="ECO:0000305"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 64..73
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 106..112
FT /evidence="ECO:0007829|PDB:1Q2L"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 138..150
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 159..173
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 177..187
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 214..225
FT /evidence="ECO:0007829|PDB:1Q2L"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 241..250
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 275..281
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 289..297
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 300..305
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 307..316
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 323..329
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 333..343
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 346..357
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 359..363
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 365..382
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 386..401
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 409..419
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:1Q2L"
FT TURN 427..432
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 439..448
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 455..459
FT /evidence="ECO:0007829|PDB:1Q2L"
FT TURN 470..472
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 475..480
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 483..494
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 524..529
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 532..537
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 545..555
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 557..560
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 563..589
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 592..612
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 613..626
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 632..648
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 653..663
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 666..668
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 672..678
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 679..681
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 684..695
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 699..707
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 710..724
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 735..737
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 743..749
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 752..754
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 756..763
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 769..787
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 789..792
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 797..799
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 801..808
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 811..823
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 825..844
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 848..862
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 869..882
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 889..898
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 902..912
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 917..925
FT /evidence="ECO:0007829|PDB:1Q2L"
FT TURN 930..932
FT /evidence="ECO:0007829|PDB:1Q2L"
FT HELIX 947..951
FT /evidence="ECO:0007829|PDB:1Q2L"
FT STRAND 956..958
FT /evidence="ECO:0007829|PDB:1Q2L"
SQ SEQUENCE 962 AA; 107708 MW; 0558C68C2F1A0540 CRC64;
MPRSTWFKAL LLLVALWAPL 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
ISAQTFADWQ KKAADIALSL PELNPYIPDD FSLIKSEKKY DHPELIVDES NLRVVYAPSR
YFASEPKADV SLILRNPKAM DSARNQVMFA LNDYLAGLAL DQLSNQASVG GISFSTNANN
GLMVNANGYT QRLPQLFQAL LEGYFSYTAT EDQLEQAKSW YNQMMDSAEK GKAFEQAIMP
AQMLSQVPYF SRDERRKILP SITLKEVLAY RDALKSGARP EFMVIGNMTE AQATTLARDV
QKQLGADGSE WCRNKDVVVD KKQSVIFEKA GNSTDSALAA VFVPTGYDEY TSSAYSSLLG
QIVQPWFYNQ LRTEEQLGYA VFAFPMSVGR QWGMGFLLQS NDKQPSFLWE RYKAFFPTAE
AKLRAMKPDE FAQIQQAVIT QMLQAPQTLG EEASKLSKDF DRGNMRFDSR DKIVAQIKLL
TPQKLADFFH QAVVEPQGMA ILSQISGSQN GKAEYVHPEG WKVWENVSAL QQTMPLMSEK
NE
