(data stored in ACNUC7421 zone)

SWISSPROT: LON1_SYNFM

ID   LON1_SYNFM              Reviewed;         815 AA.
AC   A0LEE9;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 85.
DE   RecName: Full=Lon protease 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01973};
GN   Name=lon1 {ECO:0000255|HAMAP-Rule:MF_01973};
GN   OrderedLocusNames=Sfum_0098;
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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       {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.
CC       {ECO:0000255|HAMAP-Rule:MF_01973}.
DR   EMBL; CP000478; ABK15801.1; -; Genomic_DNA.
DR   RefSeq; WP_011696974.1; NC_008554.1.
DR   SMR; A0LEE9; -.
DR   STRING; 335543.Sfum_0098; -.
DR   MEROPS; S16.001; -.
DR   EnsemblBacteria; ABK15801; ABK15801; Sfum_0098.
DR   KEGG; sfu:Sfum_0098; -.
DR   eggNOG; ENOG4105C6P; Bacteria.
DR   eggNOG; COG0466; LUCA.
DR   HOGENOM; HOG000261410; -.
DR   KO; K01338; -.
DR   OMA; PILCLYG; -.
DR   OrthoDB; 128102at2; -.
DR   BioCyc; SFUM335543:G1G7I-102-MONOMER; -.
DR   Proteomes; UP000001784; 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; A0LEE9.
DR   SWISS-2DPAGE; A0LEE9.
KW   ATP-binding; Complete proteome; Cytoplasm; Hydrolase;
KW   Nucleotide-binding; Protease; Reference proteome; Serine protease;
KW   Stress response.
FT   CHAIN         1    815       Lon protease 1.
FT                                /FTId=PRO_0000396605.
FT   DOMAIN       19    210       Lon N-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01123}.
FT   DOMAIN      601    782       Lon proteolytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01122}.
FT   NP_BIND     364    371       ATP. {ECO:0000255|HAMAP-Rule:MF_01973}.
FT   ACT_SITE    688    688       {ECO:0000255|HAMAP-Rule:MF_01973}.
FT   ACT_SITE    731    731       {ECO:0000255|HAMAP-Rule:MF_01973}.
SQ   SEQUENCE   815 AA;  91777 MW;  D0C246D66E7A5B60 CRC64;
     MFKLTRNKDE QSGSATFAMP LLPLRDIVVF PSMVVPLFVG RDKSVNALDK AMATDKKIFL
     AAQTKAKTDT PGESDIYRVG TVANILQILR LPDGTVKVLV EGDFRARISS FIPHPDHFFV
     SLEGLEESED ESVEIEALRR GVRAAFDAYS KHNKKINQEI LDAVAAIDNA SRLADTIAAY
     MPFKLDVKQK LLETLGVAKR LEKLFGQIRS EIEILQTEER IKGRVKKQME KTQREYYLNE
     QMRAIQKEMG EKDDFKSELE ELEKRIKRKK LSQEAAAKVR AEFKKLKLMS PMSAEATVVR
     NYIDWILSLP WYEKTRDKLD IDESIRILDE DHYGLEKPKE RIIEYLAVQA LVKRIKGPIL
     CFVGPPGVGK TSLAKSIARA MNRNFIRLSL GGVRDEAEIR GHRRTYIGAM PGKIIQSLKK
     VKSNNPVFCL DEVDKMSMDF RGDPSAALLE VLDPEQNFSF NDHYLDLDYD LSEVFFITTA
     NNLHSIPPPL RDRMEIIQIA GYTEFDKLNI GRNFLVAKQC KANGLSLDNI AFSDDMLLYI
     IRHYTKEAGV RNLEREIASI CRKVAKEVVR RGPETRIELT EDLVQEYLGI PKFRYGVAEE
     KDEIGLAVGL AWTEFGGDIL GIETVVMPGK GKVQITGKLG DVMQESAQAA LSYVRSRAKR
     LGIDPDFYQN FDIHVHVPEG AIPKDGPSAG ITMATSIVSA LARIPVRSDL AMTGEITLRG
     RVLPIGGLKE KILAAHRALL KTVLIPKDNA KDLKDIPAKI LEEIQVELVE HMDDVLRKAM
     VVPEDRELFH EEEAGAQQAV MFEQKPPAAD EIRAH
//

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