LON_SALAI
ID LON_SALAI Reviewed; 778 AA.
AC A8M1E8;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=Sare_2249;
OS Salinispora arenicola (strain CNS-205).
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Salinispora.
OX NCBI_TaxID=391037;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNS-205;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C.,
RA Udwary D., Xiang L., Gontang E., Richardson P.;
RT "Complete sequence of Salinispora arenicola CNS-205.";
RL Submitted (OCT-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}.
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DR EMBL; CP000850; ABV98109.1; -; Genomic_DNA.
DR RefSeq; WP_012182411.1; NC_009953.1.
DR AlphaFoldDB; A8M1E8; -.
DR SMR; A8M1E8; -.
DR STRING; 391037.Sare_2249; -.
DR PRIDE; A8M1E8; -.
DR EnsemblBacteria; ABV98109; ABV98109; Sare_2249.
DR GeneID; 5705875; -.
DR KEGG; saq:Sare_2249; -.
DR PATRIC; fig|391037.6.peg.2278; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_11; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 128102at2; -.
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..778
FT /note="Lon protease"
FT /id="PRO_0000396596"
FT DOMAIN 4..185
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 581..762
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 668
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 711
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 346..353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 778 AA; 82739 MW; C1EAF21FE7EC538B CRC64;
MATLPVLPLT DAVLLPGMAI PVTLDPTTQA AVDAARATGD QRLLAVPRLD GEYGPVGVVA
TIEKVGRLPS GEPAAVVRGL ARARIGSGVP GPGAALWVEA AELAEPAPAG RARELAREYR
ALMTSVLQQR GAWQVIDAIE RMTDLSELAD SAGYVSWLSL AQKTELLAAP DVTTRLELLV
GWVRAHLAEQ EVAEQINTDV REGLEKSQRE FLLRQQLATI RKELGEDEPE GSADYRARVE
AADLPAPVRD AALREVGKLE RASDASPEAG WIRTWLDTVL EMPWNTRTED NTDLVAARAV
LDADHAGLTD VKDRILEYLA VRNRRVERNL GVVGGRGSGA VLALAGPPGV GKTSLGESVA
RALGRRFVRV SLGGVRDEAE IRGHRRTYVG ALPGRIVRAL REAGSMNPVV LLDEVDKLAV
GYSGDPAAAL LEVLDPAQNH TFRDHYLEVD LDLSDVLFLA TANVVEAIPS PLLDRMELVT
LDGYTEDEKV AIARDHLLPR QRERAGLTAD EVTISDGVLA RIAGEYTREA GVRQLERSLA
KIFRKVAVTA TTDPAPVHVD TGNLHRYLGR PKFSPESAER TAVPGVATGL AVTGAGGDVL
FVEATSMAGE PGLTLTGQLG DVMKESAQIA LSYLRSNGRR LGLDPNALAG RRIHLHVPAG
AVPKDGPSAG ITMVTALASL VSGRPVRPEF GMTGEVTLSG RALPIGGVKQ KLLAAHRAGL
TEVIIPQRNE PDLDDLPAEV REALTVHTLA DVADVLALAL RPADLDADSL DGEALATA
