(data stored in SCRATCH zone)

SWISSPROT: LON_LACP7

ID   LON_LACP7               Reviewed;         809 AA.
AC   A9KH99;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   11-DEC-2019, entry version 84.
DE   RecName: Full=Lon protease {ECO:0000255|HAMAP-Rule:MF_01973};
DE            EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_01973};
DE   AltName: Full=ATP-dependent protease La {ECO:0000255|HAMAP-Rule:MF_01973};
GN   Name=lon {ECO:0000255|HAMAP-Rule:MF_01973}; OrderedLocusNames=Cphy_0379;
OS   Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
OS   (Clostridium phytofermentans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae.
OX   NCBI_TaxID=357809;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700394 / DSM 18823 / ISDg;
RA   Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L.,
RA   LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA   Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E.A., Richardson P.;
RT   "Complete genome sequence of Clostridium phytofermentans ISDg.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC       degradation of mutant and abnormal proteins as well as certain short-
CC       lived regulatory proteins. Required for cellular homeostasis and for
CC       survival from DNA damage and developmental changes induced by stress.
CC       Degrades polypeptides processively to yield small peptide fragments
CC       that are 5 to 10 amino acids long. Binds to DNA in a double-stranded,
CC       site-specific manner. {ECO:0000255|HAMAP-Rule:MF_01973}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01973};
CC   -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC       {ECO:0000255|HAMAP-Rule:MF_01973}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01973}.
CC   -!- INDUCTION: By heat shock. {ECO:0000255|HAMAP-Rule:MF_01973}.
CC   -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01973}.
DR   EMBL; CP000885; ABX40766.1; -; Genomic_DNA.
DR   RefSeq; WP_012198409.1; NC_010001.1.
DR   SMR; A9KH99; -.
DR   STRING; 357809.Cphy_0379; -.
DR   MEROPS; S16.001; -.
DR   PRIDE; A9KH99; -.
DR   EnsemblBacteria; ABX40766; ABX40766; Cphy_0379.
DR   KEGG; cpy:Cphy_0379; -.
DR   eggNOG; ENOG4105C6P; Bacteria.
DR   eggNOG; COG0466; LUCA.
DR   HOGENOM; HOG000261410; -.
DR   KO; K01338; -.
DR   OMA; EYFLHQQ; -.
DR   OrthoDB; 128102at2; -.
DR   BioCyc; CPHY357809:G1GAJ-426-MONOMER; -.
DR   Proteomes; UP000000370; 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   3: Inferred from homology;
DR   PRODOM; A9KH99.
DR   SWISS-2DPAGE; A9KH99.
KW   ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW   Reference proteome; Serine protease; Stress response.
FT   CHAIN           1..809
FT                   /note="Lon protease"
FT                   /id="PRO_0000396549"
FT   DOMAIN          8..201
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          629..809
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   NP_BIND         354..361
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   ACT_SITE        716
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   ACT_SITE        759
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ   SEQUENCE   809 AA;  90510 MW;  28E162BD3E1421AB CRC64;
     MSEYTRQLPV VALRNMAVMP GMLIHFDVNR KVSIEAIEAA MLLNQQVLLV SQIDAETENP
     TADDLYRVGT IAEIKQMIKL PGNVIRVLVT GLERATLDSL VSEQPYLKAQ LTSKEAELLN
     LTEAEEEAMV RALRDLFEVY TTENNKLNKD IIRQVEASRE IEKMVEQLSI HIPMTLEDKQ
     LLLAASDLME QYERLCLILA DEIEVMRIKR ELQNKVKDKV DKNQKDYIMR EQLKVIKEEL
     GETSSVSDIM QYLEQLKELV ASDEVKEKIK KEIERFQNVA GSNSESAVAR GYVETLLSLP
     WDKVSEDFMD LAYAKEVLET EHYGLKKVKE RVLDFLAVRQ LTEKGDSPII CLVGPPGTGK
     TSIARSIAKA LNKEYVRISL GGVRDEAEIR GHRRTYVGAL PGRIITGLKQ AKVKNPLMLL
     DEIDKMSSDY KGDTASAMLE VLDSEQNCNF VDHYVEIPVD LSEVMFIATA NTTQTIPKPL
     LDRMEIIEVS SYTENEKFHI AKNHLLNKQI EKNGLKKSQI SISEKALRKI ISDYTREAGV
     RGLERKISEV CRKIARELLE QESKENQNLI KSAKNKSNNK NQSHSEVAAA VEAEEISVTT
     KPSKIKVTEK NITTYLGKPK FRNEIASQKD EVGIVCGLAW TSVGGTTLQI EVNSLPGKGA
     LILTGQMGDV MKESAQLGIS YIRSLSKEYK ISEEYFQKND IHIHIPEGAT PKDGPSAGIT
     MATAMLSAIT GKKVHAKVAM TGEITLRGRV LPIGGLKEKL LAAKNTGIKK VLIPEKNRPD
     LEELEQEITE GMEVICVATM DEVLKHALV
//

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