LON_BACAH
ID LON_BACAH Reviewed; 794 AA.
AC A0RJ87;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=BALH_4063;
OS Bacillus thuringiensis (strain Al Hakam).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=412694;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Al Hakam;
RX PubMed=17337577; DOI=10.1128/jb.00241-07;
RA Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D.,
RA McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.;
RT "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL J. Bacteriol. 189:3680-3681(2007).
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}.
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DR EMBL; CP000485; ABK87280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0RJ87; -.
DR SMR; A0RJ87; -.
DR MEROPS; S16.001; -.
DR EnsemblBacteria; ABK87280; ABK87280; BALH_4063.
DR KEGG; btl:BALH_4063; -.
DR HOGENOM; CLU_004109_4_3_9; -.
DR OMA; GAWQVVD; -.
DR Proteomes; UP000000761; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; 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; 2.30.130.40; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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_prtase_N.
DR InterPro; IPR046336; Lon_prtase_N_sf.
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;
KW ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW Serine protease; Stress response.
FT CHAIN 1..794
FT /note="Lon protease"
FT /id="PRO_0000396536"
FT DOMAIN 29..220
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 610..791
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 697
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 740
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 374..381
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 794 AA; 88610 MW; 34013298AC6FE4BE CRC64;
MYCNIKWLNR SLIYYGGAMS SMNTNERIVP LLPLRGVLVY PTMVLHLDVG RDKSIQALEQ
AAMDENIIFL AMQKEMNIDD PKEDDIYSVG TVAKVKQMLK LPNGTLRVLV EGLHRAEVVE
FIEEENVVQV SIKTVTEEVE ADLEEKALMR TLLEHFEQYI KVSKKVSNET FATVADVEEP
GRLADLIASH LPIKTKQKQE ILEIISVKER LHTLISIIQD EQELLSLEKK IGQKVKRSME
RTQKEYFLRE QMKAIQTELG DKEGKGGEVE ELREKIEQSG MPEETMKAAL KELDRYEKLP
ASSAESGVIR NYMDWLLALP WTDATEDMID LAHSEEILNK DHYGLEKVKE RVLEYLAVQK
LTNSLKGPIL CLVGPPGVGK TSLARSIATS LNRNFVRVSL GGVRDESEIR GHRRTYVGAM
PGRIIQGMKK AKSVNPVFLL DEIDKMSNDF RGDPSAALLE VLDPEQNHNF SDHYIEEPYD
LSKVMFVATA NTLSSIPGPL LDRMEIISIA GYTELEKVHI AREHLLPKQL QEHGLRKGNL
QVRDEALLEI IRYYTREAGV RTLERQIAKV CRKAAKIIVT AERKRIVVTE KNVVDLLGKH
IFRYGQAEKT DQVGMATGLA YTAAGGDTLA IEVSVAPGKG KLILTGKLGD VMKESAQAAF
SYIRSRAEEL QIDPDFHEKN DIHIHVPEGA VPKDGPSAGI TMATALISAL TGIPVSKEVG
MTGEITLRGR VLPIGGLKEK TLSAHRAGLT KIILPAENEK DLDDIPESVK ENLTFVLASH
LDEVLEHALV GVKQ
