(data stored in ACNUC7421 zone)

SWISSPROT: B7UJR2_ECO27

ID   B7UJR2_ECO27            Unreviewed;       784 AA.
AC   B7UJR2;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 89.
DE   RecName: Full=Lon protease {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
DE            EC=3.4.21.53 {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
DE   AltName: Full=ATP-dependent protease La {ECO:0000256|HAMAP-Rule:MF_01973};
GN   Name=lon {ECO:0000256|HAMAP-Rule:MF_01973,
GN   ECO:0000313|EMBL:CAS07922.1};
GN   OrderedLocusNames=E2348C_0374 {ECO:0000313|EMBL:CAS07922.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07922.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07922.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: ATP-dependent serine protease that mediates the
CC       selective degradation of mutant and abnormal proteins as well as
CC       certain short-lived regulatory proteins. Required for cellular
CC       homeostasis and for survival from DNA damage and developmental
CC       changes induced by stress. Degrades polypeptides processively to
CC       yield small peptide fragments that are 5 to 10 amino acids long.
CC       Binds to DNA in a double-stranded, site-specific manner.
CC       Endogenous substrates include the regulatory proteins RcsA and
CC       SulA, the transcriptional activator SoxS, and UmuD. Its
CC       overproduction specifically inhibits translation through at least
CC       two different pathways, one of them being the YoeB-YefM toxin-
CC       antitoxin system. {ECO:0000256|HAMAP-Rule:MF_01973}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01973,
CC         ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-
CC         ProRule:PRU01122, ECO:0000256|SAAS:SAAS01117331};
CC   -!- ACTIVITY REGULATION: Contains an allosteric site (distinct from
CC       its active site), whose occupancy by an unfolded polypeptide leads
CC       to enzyme activation. {ECO:0000256|HAMAP-Rule:MF_01973}.
CC   -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC       ATP binding and hydrolysis do not affect the oligomeric state of
CC       the enzyme. {ECO:0000256|HAMAP-Rule:MF_01973}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973,
CC       ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|SAAS:SAAS00004358}.
CC   -!- INDUCTION: By accumulation of abnormal proteins, such as at high
CC       temperatures. Under stress conditions. {ECO:0000256|HAMAP-
CC       Rule:MF_01973}.
CC   -!- SIMILARITY: Belongs to the peptidase S16 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174,
CC       ECO:0000256|PROSITE-ProRule:PRU01122,
CC       ECO:0000256|RuleBase:RU000591, ECO:0000256|SAAS:SAAS00536024}.
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DR   EMBL; FM180568; CAS07922.1; -; Genomic_DNA.
DR   RefSeq; WP_001295325.1; NC_011601.1.
DR   SMR; B7UJR2; -.
DR   EnsemblBacteria; CAS07922; CAS07922; E2348C_0374.
DR   KEGG; ecg:E2348C_0374; -.
DR   HOGENOM; HOG000261408; -.
DR   KO; K01338; -.
DR   OMA; PILCLYG; -.
DR   BioCyc; ECOL574521:E2348C_RS01965-MONOMER; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0034605; P:cellular response to heat; IEA:UniProtKB-UniRule.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.230.10; -; 1.
DR   HAMAP; MF_01973; lon_bact; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR027543; Lon_bac.
DR   InterPro; IPR004815; Lon_bac/euk-typ.
DR   InterPro; IPR008269; Lon_proteolytic.
DR   InterPro; IPR027065; Lon_Prtase.
DR   InterPro; IPR003111; Lon_substr-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008268; Peptidase_S16_AS.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   PANTHER; PTHR10046; PTHR10046; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   Pfam; PF02190; LON_substr_bdg; 1.
DR   PIRSF; PIRSF001174; Lon_proteas; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00464; LON; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   TIGRFAMs; TIGR00763; lon; 1.
DR   PROSITE; PS51787; LON_N; 1.
DR   PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR   PROSITE; PS01046; LON_SER; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; B7UJR2.
DR   SWISS-2DPAGE; B7UJR2.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01973,
KW   ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PIRSR:PIRSR001174-2,
KW   ECO:0000256|RuleBase:RU000591}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973,
KW   ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|SAAS:SAAS00417288};
KW   DNA-binding {ECO:0000313|EMBL:CAS07922.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01973,
KW   ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-ProRule:PRU01122,
KW   ECO:0000256|RuleBase:RU000591};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01973,
KW   ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PIRSR:PIRSR001174-2,
KW   ECO:0000256|RuleBase:RU000591};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_01973,
KW   ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-ProRule:PRU01122,
KW   ECO:0000256|RuleBase:RU000591};
KW   Serine protease {ECO:0000256|HAMAP-Rule:MF_01973,
KW   ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-ProRule:PRU01122,
KW   ECO:0000256|RuleBase:RU000591};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_01973,
KW   ECO:0000256|SAAS:SAAS00070204}.
FT   INIT_MET      1      1       Removed. {ECO:0000256|HAMAP-Rule:
FT                                MF_01973}.
FT   DOMAIN       11    202       Lon N-terminal. {ECO:0000259|PROSITE:
FT                                PS51787}.
FT   DOMAIN      592    773       Lon proteolytic. {ECO:0000259|PROSITE:
FT                                PS51786}.
FT   NP_BIND     356    363       ATP. {ECO:0000256|HAMAP-Rule:MF_01973,
FT                                ECO:0000256|PIRSR:PIRSR001174-2}.
FT   COILED      190    227       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    679    679       {ECO:0000256|HAMAP-Rule:MF_01973,
FT                                ECO:0000256|PIRSR:PIRSR001174-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU01122}.
FT   ACT_SITE    722    722       {ECO:0000256|HAMAP-Rule:MF_01973,
FT                                ECO:0000256|PIRSR:PIRSR001174-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU01122}.
SQ   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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