(data stored in ACNUC7421 zone)

SWISSPROT: A0A152UUM3_ECO57

ID   A0A152UUM3_ECO57        Unreviewed;       784 AA.
AC   A0A152UUM3; A0A0H3JFZ2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   05-JUL-2017, entry version 11.
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   OrderedLocusNames=ECs0493 {ECO:0000313|EMBL:BAB33916.1};
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|EMBL:BAB33916.1, ECO:0000313|Proteomes:UP000000558};
RN   [1] {ECO:0000313|EMBL:BAB33916.1, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC
RC   {ECO:0000313|Proteomes:UP000000558};
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of proteins in presence of ATP.
CC       {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174,
CC       ECO:0000256|SAAS:SAAS00007438}.
CC   -!- ENZYME REGULATION: Contains an allosteric site (distinct from its
CC       active site), whose occupancy by an unfolded polypeptide leads to
CC       enzyme activation. {ECO:0000256|HAMAP-Rule:MF_01973}.
CC   -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC       {ECO:0000256|PIRNR:PIRNR001174}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973,
CC       ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|SAAS:SAAS00007367}.
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; BA000007; BAB33916.1; -; Genomic_DNA.
DR   RefSeq; NP_308520.1; NC_002695.1.
DR   RefSeq; WP_001302567.1; NZ_MWVM01000009.1.
DR   ProteinModelPortal; A0A152UUM3; -.
DR   EnsemblBacteria; BAB33916; BAB33916; BAB33916.
DR   GeneID; 914595; -.
DR   KEGG; ecs:ECs0493; -.
DR   PATRIC; fig|386585.9.peg.596; -.
DR   KO; K01338; -.
DR   Proteomes; UP000000558; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0033554; P:cellular response to stress; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006515; P:misfolded or incompletely synthesized protein catabolic process; IEA:UniProtKB-HAMAP.
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_domain.
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; A0A152UUM3.
DR   SWISS-2DPAGE; A0A152UUM3.
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:UP000000558};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973,
KW   ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|SAAS:SAAS00004285};
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:SAAS00004281}.
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;  87437 MW;  7CEE8E303BAEE257 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 NTDHYGLERV 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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