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Lon protease (EC 3.4.21.53) (ATP-dependent protease La)

 LON_ECOLI               Reviewed;         784 AA.
P0A9M0; P08177; P78219; Q2MBY7;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
19-JUL-2005, sequence version 1.
25-OCT-2017, entry version 119.
RecName: Full=Lon protease {ECO:0000255|HAMAP-Rule:MF_01973};
EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_01973};
AltName: Full=ATP-dependent protease La {ECO:0000255|HAMAP-Rule:MF_01973};
Name=lon {ECO:0000255|HAMAP-Rule:MF_01973};
Synonyms=capR, deg, lopA, muc; OrderedLocusNames=b0439, JW0429;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=8294008; DOI=10.1016/0378-1119(93)90471-E;
Thomas C.D., Modha J., Razzaq T.M., Cullis P.M., Rivett A.;
"Controlled high-level expression of the lon gene of Escherichia coli
allows overproduction of Lon protease.";
Gene 136:237-242(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3289547;
Amerik A.Y., Chistyakova L.G., Ostroumova N.I., Gurevich A.I.,
Antonov V.K.;
"Cloning, expression and structure of the functionally active
shortened lon gene in Escherichia coli.";
Bioorg. Khim. 14:408-411(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=2242054;
Amerik A.I.U., Antonov V.K., Ostroumova N.I., Rotanova T.V.,
Chistiakova L.G.;
"Cloning, structure and expression of the full-size lon gene in
Escherichia coli coding for ATP-dependent La-proteinase.";
Bioorg. Khim. 16:869-880(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF SER-679.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8226758;
Fischer H., Glockshuber R.;
"ATP hydrolysis is not stoichiometrically linked with proteolysis in
the ATP-dependent protease La from Escherichia coli.";
J. Biol. Chem. 268:22502-22507(1993).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 783-783.
PubMed=3042779;
Chin D.T., Goff S.A., Webster T., Smith T., Goldberg A.L.;
"Sequence of the lon gene in Escherichia coli. A heat-shock gene which
encodes the ATP-dependent protease La.";
J. Biol. Chem. 263:11718-11728(1988).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58, AND PROTEIN SEQUENCE OF
1-14.
PubMed=2984174;
Gayda R.C., Stephens P.E., Hewick R., Schoemaker J.M., Dreyer W.J.,
Markovitz A.;
"Regulatory region of the heat shock-inducible capR (lon) gene: DNA
and protein sequences.";
J. Bacteriol. 162:271-275(1985).
[10]
PROTEIN SEQUENCE OF 2-9, AND DNA-BINDING.
STRAIN=ATCC 37196 / Y1089;
PubMed=8995294; DOI=10.1074/jbc.272.41.25678;
Fu G.K., Smith M.J., Markovitz D.M.;
"Bacterial protease Lon is a site-specific DNA-binding protein.";
J. Biol. Chem. 272:534-538(1997).
[11]
MUTAGENESIS OF LYS-362.
PubMed=7988699; DOI=10.1016/0014-5793(94)01244-X;
Fischer H., Glockshuber R.;
"A point mutation within the ATP-binding site inactivates both
catalytic functions of the ATP-dependent protease La (Lon) from
Escherichia coli.";
FEBS Lett. 356:101-103(1994).
[12]
CLEAVAGE OF CCDA ANTITOXIN.
STRAIN=K12;
PubMed=8022284; DOI=10.1111/j.1365-2958.1994.tb00391.x;
Van Melderen L., Bernard P., Couturier M.;
"Lon-dependent proteolysis of CcdA is the key control for activation
of CcdB in plasmid-free segregant bacteria.";
Mol. Microbiol. 11:1151-1157(1994).
[13]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[14]
MUTAGENESIS OF HIS-665; HIS-667; ASP-676 AND ASP-743.
PubMed=9490010; DOI=10.1016/S0014-5793(98)00012-X;
Starkova N.N., Koroleva E.P., Rumsh L.D., Ginodman L.M.,
Rotanova T.V.;
"Mutations in the proteolytic domain of Escherichia coli protease Lon
impair the ATPase activity of the enzyme.";
FEBS Lett. 422:218-220(1998).
[15]
CLEAVAGE OF UMUD.
PubMed=9869642; DOI=10.1101/gad.12.24.3889;
Gonzalez M., Frank E.G., Levine A.S., Woodgate R.;
"Lon-mediated proteolysis of the Escherichia coli UmuD mutagenesis
protein: in vitro degradation and identification of residues required
for proteolysis.";
Genes Dev. 12:3889-3899(1998).
[16]
MUTAGENESIS.
PubMed=10094703;
Ebel W., Skinner M.M., Dierksen K.P., Scott J.M., Trempy J.E.;
"A conserved domain in Escherichia coli Lon protease is involved in
substrate discriminator activity.";
J. Bacteriol. 181:2236-2243(1999).
[17]
FUNCTION.
PubMed=12135363; DOI=10.1021/bi0255470;
Thomas-Wohlever J., Lee I.;
"Kinetic characterization of the peptidase activity of Escherichia
coli Lon reveals the mechanistic similarities in ATP-dependent
hydrolysis of peptide and protein substrates.";
Biochemistry 41:9418-9425(2002).
[18]
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=15560777; DOI=10.1111/j.1432-1033.2004.04421.x;
Besche H., Zwickl P.;
"The Thermoplasma acidophilum Lon protease has a Ser-Lys dyad active
site.";
Eur. J. Biochem. 271:4361-4365(2004).
[19]
INTERACTION WITH THE YOEB-YEFM TOXIN-ANTITOXIN SYSTEM.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15009896; DOI=10.1046/j.1365-2958.2003.03941.x;
Christensen S.K., Maenhaut-Michel G., Mine N., Gottesman S.,
Gerdes K., Van Melderen L.;
"Overproduction of the Lon protease triggers inhibition of translation
in Escherichia coli: involvement of the yefM-yoeB toxin-antitoxin
system.";
Mol. Microbiol. 51:1705-1717(2004).
[20]
FUNCTION.
PubMed=16584195; DOI=10.1021/bi052377t;
Vineyard D., Patterson-Ward J., Lee I.;
"Single-turnover kinetic experiments confirm the existence of
high- and low-affinity ATPase sites in Escherichia coli Lon
protease.";
Biochemistry 45:4602-4610(2006).
[21]
CLEAVAGE OF SOXS.
PubMed=16460757; DOI=10.1016/j.jmb.2005.12.088;
Shah I.M., Wolf R.E. Jr.;
"Sequence requirements for Lon-dependent degradation of the
Escherichia coli transcription activator SoxS: identification of the
SoxS residues critical to proteolysis and specific inhibition of in
vitro degradation by a peptide comprised of the N-terminal 21 amino
acid residues.";
J. Mol. Biol. 357:718-731(2006).
[22]
SUBUNIT.
PubMed=16511355;
Park S.C., Jia B., Yang J.K., Van D.L., Shao Y.G., Han S.W.,
Jeon Y.J., Chung C.H., Cheong G.W.;
"Oligomeric structure of the ATP-dependent protease La (Lon) of
Escherichia coli.";
Mol. Cells 21:129-134(2006).
[23]
ROLE IN REGULATION OF OMPF IN ASSOCIATION WITH YCGE, AND DISRUPTION
PHENOTYPE.
STRAIN=K12 / AG100;
PubMed=19721064; DOI=10.1128/AAC.00787-09;
Duval V., Nicoloff H., Levy S.B.;
"Combined inactivation of lon and ycgE decreases multidrug
susceptibility by reducing the amount of OmpF porin in Escherichia
coli.";
Antimicrob. Agents Chemother. 53:4944-4948(2009).
[24]
FUNCTION IN PERSISTENCE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
LYS-362 AND SER-679.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=21788497; DOI=10.1073/pnas.1100186108;
Maisonneuve E., Shakespeare L.J., Joergensen M.G., Gerdes K.;
"Bacterial persistence by RNA endonucleases.";
Proc. Natl. Acad. Sci. U.S.A. 108:13206-13211(2011).
[25]
CLEAVAGE OF HIPB ANTITOXIN.
PubMed=22720069; DOI=10.1371/journal.pone.0039185;
Hansen S., Vulic M., Min J., Yen T.J., Schumacher M.A., Brennan R.G.,
Lewis K.;
"Regulation of the Escherichia coli HipBA toxin-antitoxin system by
proteolysis.";
PLoS ONE 7:E39185-E39185(2012).
[26]
CLEAVAGE OF ANTITOXIN MAZE, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / BW25113, and K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=24375411; DOI=10.1074/jbc.M113.510511;
Tripathi A., Dewan P.C., Siddique S.A., Varadarajan R.;
"MazF-induced growth inhibition and persister generation in
Escherichia coli.";
J. Biol. Chem. 289:4191-4205(2014).
[27]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 585-784, AND ACTIVE SITE
LYS-722.
PubMed=14665623; DOI=10.1074/jbc.M312243200;
Botos I., Melnikov E.E., Cherry S., Tropea J.E., Khalatova A.G.,
Rasulova F., Dauter Z., Maurizi M.R., Rotanova T.V., Wlodawer A.,
Gustchina A.;
"The catalytic domain of Escherichia coli Lon protease has a unique
fold and a Ser-Lys dyad in the active site.";
J. Biol. Chem. 279:8140-8148(2004).
[28]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 491-584.
PubMed=15037242; DOI=10.1016/j.jsb.2003.09.003;
Botos I., Melnikov E.E., Cherry S., Khalatova A.G., Rasulova F.S.,
Tropea J.E., Maurizi M.R., Rotanova T.V., Gustchina A., Wlodawer A.;
"Crystal structure of the AAA+ alpha domain of E. coli Lon protease at
1.9A resolution.";
J. Struct. Biol. 146:113-122(2004).
[29]
X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 1-118.
PubMed=16199667; DOI=10.1110/ps.051736805;
Li M., Rasulova F., Melnikov E.E., Rotanova T.V., Gustchina A.,
Maurizi M.R., Wlodawer A.;
"Crystal structure of the N-terminal domain of E. coli Lon protease.";
Protein Sci. 14:2895-2900(2005).
-!- FUNCTION: ATP-dependent serine protease that mediates the
selective degradation of mutant and abnormal proteins as well as
certain short-lived regulatory proteins, including some
antitoxins. Required for cellular homeostasis and for survival
from DNA damage and developmental changes induced by stress.
Degrades polypeptides processively to yield small peptide
fragments that are 5 to 10 amino acids long. Binds to DNA in a
double-stranded, site-specific manner. Endogenous substrates
include the regulatory proteins RcsA and SulA, the transcriptional
activator SoxS, UmuD and at least type II antitoxins CcdA, HipB
and MazE (PubMed:8022284, PubMed:16460757, PubMed:22720069,
PubMed:24375411). Its overproduction specifically inhibits
translation through at least two different pathways, one of them
being the YoeB-YefM toxin-antitoxin system (PubMed:15009896).
Overproduction leads to very high persister cell formation (cells
highly resistant to antibiotics), but not when 10 mRNA
interferases are deleted, nor when Lon catalytic residues are
mutated (PubMed:21788497). {ECO:0000269|PubMed:12135363,
ECO:0000269|PubMed:15009896, ECO:0000269|PubMed:16460757,
ECO:0000269|PubMed:16584195, ECO:0000269|PubMed:19721064,
ECO:0000269|PubMed:21788497, ECO:0000269|PubMed:22720069,
ECO:0000269|PubMed:24375411, ECO:0000269|PubMed:8022284}.
-!- CATALYTIC ACTIVITY: Hydrolysis of proteins in presence of ATP.
{ECO:0000255|HAMAP-Rule:MF_01973}.
-!- ENZYME REGULATION: Contains an allosteric site (distinct from its
active site), whose occupancy by an unfolded polypeptide leads to
enzyme activation.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.201 mM for ATP for ATPase activity
{ECO:0000269|PubMed:15560777};
-!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
ATP binding and hydrolysis do not affect the oligomeric state of
the enzyme. {ECO:0000255|HAMAP-Rule:MF_01973,
ECO:0000269|PubMed:16511355}.
-!- INTERACTION:
P0A7R1:rplI; NbExp=4; IntAct=EBI-547203, EBI-546437;
P33225:torA; NbExp=2; IntAct=EBI-547203, EBI-557008;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- INDUCTION: By accumulation of abnormal proteins, such as at high
temperatures. Under stress conditions.
-!- DISRUPTION PHENOTYPE: When both lon and ycgE are disrupted levels
of OmpF decrease, leading to lower drug susceptibility, with a
greater effect at 26 degrees than at 37 degrees Celsius. The
mechanism is not yet understood (PubMed:19721064). Decreased
persister cell formation upon antibiotic challenge due probably
due to increased levels of MazF toxin (PubMed:24375411). Decreased
persister cell formation, further reduced when 10 mRNA toxin
interferases are also deleted (PubMed:21788497).
{ECO:0000269|PubMed:19721064, ECO:0000269|PubMed:21788497,
ECO:0000269|PubMed:24375411}.
-!- MISCELLANEOUS: Both its proteolytic and protein-activated ATPase
activities are stimulated by DNA, especially single-stranded DNA.
-!- MISCELLANEOUS: Both high- and low-affinity ATPase sites are
present in the homooligomer. Optimal peptidase activity requires
ATP binding and hydrolysis at both sites, but ATP hydrolysis is
not stoichiometrically linked to peptide hydrolysis.
-!- SIMILARITY: Belongs to the peptidase S16 family.
{ECO:0000255|HAMAP-Rule:MF_01973}.
-!- SEQUENCE CAUTION:
Sequence=AAA23537.1; Type=Frameshift; Positions=16; Evidence={ECO:0000305};
Sequence=AAB40195.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; L12349; AAC36871.1; -; Unassigned_DNA.
EMBL; M38347; AAA24079.1; -; Genomic_DNA.
EMBL; L20572; AAA16837.1; -; Unassigned_DNA.
EMBL; J03896; AAA24078.1; -; Genomic_DNA.
EMBL; U82664; AAB40195.1; ALT_INIT; Genomic_DNA.
EMBL; U00096; AAC73542.1; -; Genomic_DNA.
EMBL; AP009048; BAE76219.1; -; Genomic_DNA.
EMBL; M10153; AAA23537.1; ALT_FRAME; Genomic_DNA.
PIR; A23101; A23101.
PIR; G64773; SUECLA.
RefSeq; NP_414973.1; NC_000913.3.
RefSeq; WP_001295325.1; NZ_LN832404.1.
PDB; 1QZM; X-ray; 1.90 A; A=491-584.
PDB; 1RR9; X-ray; 2.10 A; A/B/C/D/E/F=585-784.
PDB; 1RRE; X-ray; 1.75 A; A/B/C/D/E/F=585-784.
PDB; 2ANE; X-ray; 2.03 A; A/B/C/D/E/F/G/H=1-118.
PDB; 3LJC; X-ray; 2.60 A; A=1-245.
PDBsum; 1QZM; -.
PDBsum; 1RR9; -.
PDBsum; 1RRE; -.
PDBsum; 2ANE; -.
PDBsum; 3LJC; -.
ProteinModelPortal; P0A9M0; -.
SMR; P0A9M0; -.
BioGrid; 4260734; 166.
DIP; DIP-35845N; -.
IntAct; P0A9M0; 72.
MINT; MINT-1224190; -.
STRING; 316385.ECDH10B_0395; -.
MEROPS; S16.001; -.
PaxDb; P0A9M0; -.
PRIDE; P0A9M0; -.
EnsemblBacteria; AAC73542; AAC73542; b0439.
EnsemblBacteria; BAE76219; BAE76219; BAE76219.
GeneID; 945085; -.
KEGG; ecj:JW0429; -.
KEGG; eco:b0439; -.
PATRIC; fig|1411691.4.peg.1837; -.
EchoBASE; EB0537; -.
EcoGene; EG10542; lon.
eggNOG; ENOG4105C6P; Bacteria.
eggNOG; COG0466; LUCA.
HOGENOM; HOG000261408; -.
InParanoid; P0A9M0; -.
KO; K01338; -.
PhylomeDB; P0A9M0; -.
BioCyc; EcoCyc:EG10542-MONOMER; -.
BioCyc; MetaCyc:EG10542-MONOMER; -.
BRENDA; 3.4.21.53; 2026.
EvolutionaryTrace; P0A9M0; -.
PRO; PR:P0A9M0; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0005524; F:ATP binding; IDA:EcoCyc.
GO; GO:0004176; F:ATP-dependent peptidase activity; IDA:EcoliWiki.
GO; GO:0016887; F:ATPase activity; IDA:EcoliWiki.
GO; GO:0003677; F:DNA binding; IDA:EcoliWiki.
GO; GO:0008233; F:peptidase activity; IDA:EcoliWiki.
GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
GO; GO:0004252; F:serine-type endopeptidase activity; IMP:EcoliWiki.
GO; GO:0006515; P:protein quality control by the ubiquitin-proteasome system; IMP:EcoCyc.
GO; GO:0006508; P:proteolysis; IDA:EcoliWiki.
GO; GO:0009408; P:response to heat; IEP:EcoliWiki.
GO; GO:0010165; P:response to X-ray; IMP:EcoCyc.
Gene3D; 3.30.230.10; -; 1.
HAMAP; MF_01973; lon_bact; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR027543; Lon_bac.
InterPro; IPR004815; Lon_bac/euk-typ.
InterPro; IPR008269; Lon_proteolytic.
InterPro; IPR027065; Lon_Prtase.
InterPro; IPR003111; Lon_substr-bd.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008268; Peptidase_S16_AS.
InterPro; IPR015947; PUA-like_domain.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
PANTHER; PTHR10046; PTHR10046; 1.
Pfam; PF00004; AAA; 1.
Pfam; PF05362; Lon_C; 1.
Pfam; PF02190; LON_substr_bdg; 1.
PIRSF; PIRSF001174; Lon_proteas; 1.
SMART; SM00382; AAA; 1.
SMART; SM00464; LON; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF88697; SSF88697; 1.
TIGRFAMs; TIGR00763; lon; 1.
PROSITE; PS51787; LON_N; 1.
PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PROSITE; PS01046; LON_SER; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Cytoplasm;
Direct protein sequencing; Hydrolase; Nucleotide-binding; Protease;
Reference proteome; Serine protease; Stress response.
INIT_MET 1 1 Removed. {ECO:0000255|HAMAP-
Rule:MF_01973,
ECO:0000269|PubMed:8995294}.
CHAIN 2 784 Lon protease.
/FTId=PRO_0000076133.
DOMAIN 11 202 Lon N-terminal. {ECO:0000255|PROSITE-
ProRule:PRU01123}.
DOMAIN 592 773 Lon proteolytic. {ECO:0000255|PROSITE-
ProRule:PRU01122}.
NP_BIND 356 363 ATP. {ECO:0000255|HAMAP-Rule:MF_01973}.
COMPBIAS 211 219 Arg/Lys-rich (basic).
COMPBIAS 240 252 Asp/Glu-rich (acidic).
COMPBIAS 255 270 Arg/Lys-rich (basic).
ACT_SITE 679 679
ACT_SITE 722 722 {ECO:0000255|HAMAP-Rule:MF_01973,
ECO:0000269|PubMed:14665623}.
MUTAGEN 362 362 K->A: Loss of proteolytic activity and
ATP-binding. No increased persister cell
formation. {ECO:0000269|PubMed:21788497,
ECO:0000269|PubMed:7988699}.
MUTAGEN 665 665 H->Y: Loss of proteolytic activity.
{ECO:0000269|PubMed:9490010}.
MUTAGEN 667 667 H->Y: Loss of proteolytic activity.
{ECO:0000269|PubMed:9490010}.
MUTAGEN 676 676 D->N: Loss of proteolytic activity.
{ECO:0000269|PubMed:9490010}.
MUTAGEN 679 679 S->A: Loss of proteolytic activity. No
increased persister cell formation.
{ECO:0000269|PubMed:21788497,
ECO:0000269|PubMed:8226758}.
MUTAGEN 743 743 D->N: No effect.
{ECO:0000269|PubMed:9490010}.
CONFLICT 264 317 PKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWN
ARSKVKKDLRQAQ -> RKRQKRKRTGVAEAENDVSDVGRS
DRSAWLYRLDGTGAVECAYEGQKRPASGA (in Ref. 5;
AAA24078). {ECO:0000305}.
CONFLICT 273 273 A -> R (in Ref. 4; AAA16837).
{ECO:0000305}.
CONFLICT 307 307 S -> T (in Ref. 4; AAA16837).
{ECO:0000305}.
CONFLICT 539 563 AGVRGLEREISKLCRKAVKQLLLDK -> RACVVWSVKSPN
CVAKRLSSYCSIT (in Ref. 5; AAA24078).
{ECO:0000305}.
CONFLICT 772 772 Q -> R (in Ref. 4; AAA16837).
{ECO:0000305}.
CONFLICT 779 784 QVVTAK -> HHSLRRRCSTASTYYWAKS (in Ref. 2;
AAA24079). {ECO:0000305}.
STRAND 9 18 {ECO:0000244|PDB:2ANE}.
STRAND 26 31 {ECO:0000244|PDB:2ANE}.
HELIX 34 44 {ECO:0000244|PDB:2ANE}.
TURN 45 47 {ECO:0000244|PDB:2ANE}.
STRAND 48 55 {ECO:0000244|PDB:2ANE}.
HELIX 65 67 {ECO:0000244|PDB:2ANE}.
STRAND 70 82 {ECO:0000244|PDB:2ANE}.
STRAND 88 105 {ECO:0000244|PDB:2ANE}.
STRAND 107 116 {ECO:0000244|PDB:2ANE}.
HELIX 124 145 {ECO:0000244|PDB:3LJC}.
HELIX 150 155 {ECO:0000244|PDB:3LJC}.
HELIX 162 171 {ECO:0000244|PDB:3LJC}.
HELIX 177 185 {ECO:0000244|PDB:3LJC}.
HELIX 189 242 {ECO:0000244|PDB:3LJC}.
HELIX 495 504 {ECO:0000244|PDB:1QZM}.
HELIX 506 513 {ECO:0000244|PDB:1QZM}.
TURN 518 520 {ECO:0000244|PDB:1QZM}.
STRAND 521 523 {ECO:0000244|PDB:1QZM}.
HELIX 525 535 {ECO:0000244|PDB:1QZM}.
STRAND 539 541 {ECO:0000244|PDB:1QZM}.
HELIX 542 560 {ECO:0000244|PDB:1QZM}.
STRAND 568 570 {ECO:0000244|PDB:1QZM}.
TURN 572 574 {ECO:0000244|PDB:1QZM}.
HELIX 575 579 {ECO:0000244|PDB:1QZM}.
STRAND 596 604 {ECO:0000244|PDB:1RRE}.
STRAND 607 619 {ECO:0000244|PDB:1RRE}.
STRAND 624 630 {ECO:0000244|PDB:1RRE}.
HELIX 632 647 {ECO:0000244|PDB:1RRE}.
HELIX 649 652 {ECO:0000244|PDB:1RRE}.
TURN 656 660 {ECO:0000244|PDB:1RRE}.
STRAND 661 667 {ECO:0000244|PDB:1RRE}.
STRAND 675 678 {ECO:0000244|PDB:1RRE}.
HELIX 681 693 {ECO:0000244|PDB:1RRE}.
STRAND 701 703 {ECO:0000244|PDB:1RRE}.
STRAND 712 714 {ECO:0000244|PDB:1RRE}.
HELIX 719 728 {ECO:0000244|PDB:1RRE}.
STRAND 733 737 {ECO:0000244|PDB:1RRE}.
HELIX 738 746 {ECO:0000244|PDB:1RRE}.
HELIX 749 754 {ECO:0000244|PDB:1RRE}.
STRAND 755 762 {ECO:0000244|PDB:1RRE}.
HELIX 763 770 {ECO:0000244|PDB:1RRE}.
STRAND 771 773 {ECO:0000244|PDB:1RRE}.
SEQUENCE 784 AA; 87438 MW; 4042499C97694EF8 CRC64;
MNPERSERIE IPVLPLRDVV VYPHMVIPLF VGREKSIRCL EAAMDHDKKI MLVAQKEAST
DEPGVNDLFT VGTVASILQM LKLPDGTVKV LVEGLQRARI SALSDNGEHF SAKAEYLESP
TIDEREQEVL VRTAISQFEG YIKLNKKIPP EVLTSLNSID DPARLADTIA AHMPLKLADK
QSVLEMSDVN ERLEYLMAMM ESEIDLLQVE KRIRNRVKKQ MEKSQREYYL NEQMKAIQKE
LGEMDDAPDE NEALKRKIDA AKMPKEAKEK AEAELQKLKM MSPMSAEATV VRGYIDWMVQ
VPWNARSKVK KDLRQAQEIL DTDHYGLERV KDRILEYLAV QSRVNKIKGP ILCLVGPPGV
GKTSLGQSIA KATGRKYVRM ALGGVRDEAE IRGHRRTYIG SMPGKLIQKM AKVGVKNPLF
LLDEIDKMSS DMRGDPASAL LEVLDPEQNV AFSDHYLEVD YDLSDVMFVA TSNSMNIPAP
LLDRMEVIRL SGYTEDEKLN IAKRHLLPKQ IERNALKKGE LTVDDSAIIG IIRYYTREAG
VRGLEREISK LCRKAVKQLL LDKSLKHIEI NGDNLHDYLG VQRFDYGRAD NENRVGQVTG
LAWTEVGGDL LTIETACVPG KGKLTYTGSL GEVMQESIQA ALTVVRARAE KLGINPDFYE
KRDIHVHVPE GATPKDGPSA GIAMCTALVS CLTGNPVRAD VAMTGEITLR GQVLPIGGLK
EKLLAAHRGG IKTVLIPFEN KRDLEEIPDN VIADLDIHPV KRIEEVLTLA LQNEPSGMQV
VTAK


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