DEGQ_ECOLI
ID DEGQ_ECOLI Reviewed; 455 AA.
AC P39099; Q2M8X9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Periplasmic pH-dependent serine endoprotease DegQ;
DE EC=3.4.21.107;
DE AltName: Full=Protease Do;
DE Flags: Precursor;
GN Name=degQ; Synonyms=hhoA; OrderedLocusNames=b3234, JW3203;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Bass S., Gu Q., Goddard A.;
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-32, FUNCTION AS A
RP SERINE PROTEASE, SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND
RP NOMENCLATURE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8576051; DOI=10.1128/jb.178.4.1146-1153.1996;
RA Waller P.R., Sauer R.T.;
RT "Characterization of degQ and degS, Escherichia coli genes encoding
RT homologs of the DegP protease.";
RL J. Bacteriol. 178:1146-1153(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).
RN [5]
RP FUNCTION AS A SERINE PROTEASE, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX PubMed=8830688; DOI=10.1128/jb.178.20.5925-5929.1996;
RA Kolmar H., Waller P.R., Sauer R.T.;
RT "The DegP and DegQ periplasmic endoproteases of Escherichia coli:
RT specificity for cleavage sites and substrate conformation.";
RL J. Bacteriol. 178:5925-5929(1996).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 28-264 IN COMPLEX WITH SUBSTRATE
RP ANALOGS, REACTION MECHANISM, MUTAGENESIS OF SER-187; ARG-191 AND ARG-329,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND ACTIVE SITE.
RX PubMed=21685389; DOI=10.1074/jbc.m111.243832;
RA Sawa J., Malet H., Krojer T., Canellas F., Ehrmann M., Clausen T.;
RT "Molecular adaptation of the DegQ protease to exert protein quality control
RT in the bacterial cell envelope.";
RL J. Biol. Chem. 286:30680-30690(2011).
CC -!- FUNCTION: DegQ could degrade transiently denatured and unfolded
CC proteins which accumulate in the periplasm following stress conditions.
CC DegQ is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a
CC preference for a beta-branched side chain amino acids. Only unfolded
CC proteins devoid of disulfide bonds appear capable to be cleaved,
CC thereby preventing non-specific proteolysis of folded proteins. DegQ
CC can substitute for the periplasmic protease DegP.
CC {ECO:0000269|PubMed:8576051, ECO:0000269|PubMed:8830688}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Acts on substrates that are at least partially unfolded. The
CC cleavage site P1 residue is normally between a pair of hydrophobic
CC residues, such as Val-|-Val.; EC=3.4.21.107;
CC -!- ACTIVITY REGULATION: Inhibited by diisopropylfluorophosphate (DFP).
CC {ECO:0000269|PubMed:8576051}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5. The degradation is efficient at pH values between
CC 4.5 and 6. {ECO:0000269|PubMed:21685389};
CC -!- SUBUNIT: DegQ can reversibly switch between different oligomeric forms
CC that represent inactive (6-mer) and active (12- and 24-mer) protease
CC states. Substrate binding triggers the conversion of the resting DegQ
CC trimer and hexamer into catalytically active 12- and 24-mers. The
CC conversion of 6-mer (DegQ6) into 12-mer (DegQ12) or 24-mer (DegQ24) is
CC crucial in regulating protease activity. {ECO:0000269|PubMed:21685389,
CC ECO:0000269|PubMed:8830688}.
CC -!- INTERACTION:
CC P39099; P39099: degQ; NbExp=6; IntAct=EBI-554733, EBI-554733;
CC P39099; P0A910: ompA; NbExp=2; IntAct=EBI-554733, EBI-371347;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:8576051}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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DR EMBL; U15661; AAC43992.1; -; Genomic_DNA.
DR EMBL; U32495; AAC44005.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58036.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76266.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77277.1; -; Genomic_DNA.
DR PIR; JC6051; JC6051.
DR RefSeq; NP_417701.1; NC_000913.3.
DR RefSeq; WP_001295271.1; NZ_STEB01000012.1.
DR PDB; 3STI; X-ray; 2.60 A; A/B/C=28-264.
DR PDB; 3STJ; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L=28-364.
DR PDB; 4A8A; EM; 14.20 A; A/B/C/D/E/F/G/H/I/J/K/L=28-455.
DR PDB; 4A8B; EM; 13.00 A; A/B/C/D/E/F/G/H/I/J/K/L=28-455.
DR PDB; 4A8C; EM; 7.50 A; A/B/C/D/E/F/G/H/I/J/K/L=28-455.
DR PDB; 4A9G; EM; 7.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/Y=28-455.
DR PDBsum; 3STI; -.
DR PDBsum; 3STJ; -.
DR PDBsum; 4A8A; -.
DR PDBsum; 4A8B; -.
DR PDBsum; 4A8C; -.
DR PDBsum; 4A9G; -.
DR AlphaFoldDB; P39099; -.
DR SMR; P39099; -.
DR BioGRID; 4261912; 37.
DR DIP; DIP-9424N; -.
DR IntAct; P39099; 10.
DR STRING; 511145.b3234; -.
DR MEROPS; S01.274; -.
DR MoonProt; P39099; -.
DR SWISS-2DPAGE; P39099; -.
DR jPOST; P39099; -.
DR PaxDb; P39099; -.
DR PRIDE; P39099; -.
DR EnsemblBacteria; AAC76266; AAC76266; b3234.
DR EnsemblBacteria; BAE77277; BAE77277; BAE77277.
DR GeneID; 66672870; -.
DR GeneID; 947812; -.
DR KEGG; ecj:JW3203; -.
DR KEGG; eco:b3234; -.
DR PATRIC; fig|1411691.4.peg.3494; -.
DR EchoBASE; EB2496; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_1_6; -.
DR InParanoid; P39099; -.
DR OMA; IIGINRQ; -.
DR PhylomeDB; P39099; -.
DR BioCyc; EcoCyc:G7682-MON; -.
DR BioCyc; MetaCyc:G7682-MON; -.
DR BRENDA; 3.4.21.107; 2165.
DR PRO; PR:P39099; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008233; F:peptidase activity; IDA:EcoliWiki.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IDA:UniProtKB.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011782; Pept_S1C_Do.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; SSF50156; 2.
DR SUPFAM; SSF50494; SSF50494; 1.
DR TIGRFAMs; TIGR02037; degP_htrA_DO; 1.
DR PROSITE; PS50106; PDZ; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Periplasm; Protease;
KW Reference proteome; Repeat; Serine protease; Signal; Stress response.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:8576051"
FT CHAIN 28..455
FT /note="Periplasmic pH-dependent serine endoprotease DegQ"
FT /id="PRO_0000026937"
FT DOMAIN 258..349
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 355..447
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ACT_SITE 109
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:21685389"
FT ACT_SITE 139
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:21685389"
FT ACT_SITE 214
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:21685389"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 212..214
FT /ligand="substrate"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21685389"
FT BINDING 230..234
FT /ligand="substrate"
FT BINDING 269..273
FT /ligand="substrate"
FT MUTAGEN 187
FT /note="S->A: Loss of peptidase activity."
FT /evidence="ECO:0000269|PubMed:21685389"
FT MUTAGEN 191
FT /note="R->A: Reduces the peptidase activity."
FT /evidence="ECO:0000269|PubMed:21685389"
FT MUTAGEN 329
FT /note="R->A: Reduces the peptidase activity."
FT /evidence="ECO:0000269|PubMed:21685389"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:3STI"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:3STI"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:3STI"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:3STI"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:3STI"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:3STI"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:3STI"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:3STI"
FT STRAND 126..135
FT /evidence="ECO:0007829|PDB:3STI"
FT TURN 136..139
FT /evidence="ECO:0007829|PDB:3STI"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:3STI"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:3STI"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:3STI"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:3STI"
FT STRAND 180..188
FT /evidence="ECO:0007829|PDB:3STI"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:3STJ"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:3STI"
FT TURN 211..215
FT /evidence="ECO:0007829|PDB:3STI"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:3STI"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:3STI"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:3STI"
FT HELIX 248..264
FT /evidence="ECO:0007829|PDB:3STI"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:3STJ"
FT HELIX 278..283
FT /evidence="ECO:0007829|PDB:3STJ"
FT STRAND 290..297
FT /evidence="ECO:0007829|PDB:3STJ"
FT HELIX 302..306
FT /evidence="ECO:0007829|PDB:3STJ"
FT HELIX 325..333
FT /evidence="ECO:0007829|PDB:3STJ"
FT STRAND 340..347
FT /evidence="ECO:0007829|PDB:3STJ"
FT STRAND 350..357
FT /evidence="ECO:0007829|PDB:3STJ"
SQ SEQUENCE 455 AA; 47205 MW; 6A090F93AC021C83 CRC64;
MKKQTQLLSA LALSVGLTLS ASFQAVASIP GQVADQAPLP SLAPMLEKVL PAVVSVRVEG
TASQGQKIPE EFKKFFGDDL PDQPAQPFEG LGSGVIINAS KGYVLTNNHV INQAQKISIQ
LNDGREFDAK LIGSDDQSDI ALLQIQNPSK LTQIAIADSD KLRVGDFAVA VGNPFGLGQT
ATSGIVSALG RSGLNLEGLE NFIQTDASIN RGNSGGALLN LNGELIGINT AILAPGGGSV
GIGFAIPSNM ARTLAQQLID FGEIKRGLLG IKGTEMSADI AKAFNLDVQR GAFVSEVLPG
SGSAKAGVKA GDIITSLNGK PLNSFAELRS RIATTEPGTK VKLGLLRNGK PLEVEVTLDT
STSSSASAEM ITPALEGATL SDGQLKDGGK GIKIDEVVKG SPAAQAGLQK DDVIIGVNRD
RVNSIAEMRK VLAAKPAIIA LQIVRGNESI YLLMR
