ID I9DUC0_9ALTE Unreviewed; 798 AA.
AC I9DUC0;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 66.
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 ORFNames=AGRI_06467 {ECO:0000313|EMBL:EIW89725.1};
OS Alishewanella agri BL06.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alishewanella.
OX NCBI_TaxID=1195246 {ECO:0000313|EMBL:EIW89725.1, ECO:0000313|Proteomes:UP000035062};
RN [1] {ECO:0000313|EMBL:EIW89725.1, ECO:0000313|Proteomes:UP000035062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL06 {ECO:0000313|EMBL:EIW89725.1,
RC ECO:0000313|Proteomes:UP000035062};
RX PubMed=22933763; DOI=10.1128/JB.01129-12;
RA Kim J., Jung J., Sung J.S., Chun J., Park W.;
RT "Genome Sequence of Pectin-Degrading Alishewanella agri, Isolated from
RT Landfill Soil.";
RL J. Bacteriol. 194:5135-5136(2012).
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:0000256|HAMAP-Rule:MF_01973}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01973,
CC ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-ProRule:PRU01122};
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}.
CC -!- INDUCTION: By heat shock. {ECO:0000256|HAMAP-Rule:MF_01973}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|HAMAP-
CC Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-
CC ProRule:PRU01122, ECO:0000256|RuleBase:RU000591}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIW89725.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKKU01000011; EIW89725.1; -; Genomic_DNA.
DR RefSeq; WP_008984195.1; NZ_AKKU01000011.1.
DR AlphaFoldDB; I9DUC0; -.
DR STRING; 1195246.AGRI_06467; -.
DR MEROPS; S16.001; -.
DR PATRIC; fig|1195246.3.peg.1279; -.
DR eggNOG; COG0466; Bacteria.
DR Proteomes; UP000035062; Unassembled WGS sequence.
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 CDD; cd19500; RecA-like_Lon; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.5.5270; -; 1.
DR Gene3D; 1.20.58.1480; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 2.30.130.40; LON domain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00763; lon; 1.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF56; LON PROTEASE; 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 PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01973};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01973,
KW ECO:0000256|PIRNR:PIRNR001174};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01973};
KW Reference proteome {ECO:0000313|Proteomes:UP000035062};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_01973};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_01973}.
FT DOMAIN 11..202
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 592..773
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 679
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT ACT_SITE 722
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT BINDING 356..363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PIRSR:PIRSR001174-2"
SQ SEQUENCE 798 AA; 88650 MW; D127948A1278B0BF CRC64;
MTTEHQETLH MPVLALRDVV VYPHMVIPLF VGRAKSIKCL DAAMDNDKQI FLVAQKDATL
DDPTEKDLYQ IGTVATILQL LKLPDGTVKV LVEGGKRAKL SKFTETKDSF AAFVELVPTQ
DIDSREQEVF LRSAINQFEG YIKLNKKIPP EVLTALSGID DAARLADTMA AHMPLKVEDK
QKVLELTDVT ARLEYLMAMM ESEIDILQVE RRIRSRVKKQ MEKSQREYYL NEQMKAIQRE
LGELEDAPDE FETLSKKIAE AKMPAEAEAK AKAELQKLKM MSPMSAEATV VRSYIDWLTQ
VPWQTRSKVK KNLAAAEQIL NADHYGLEKV KERIMEYLAV QQRVNKLKGP ILCLVGPPGV
GKTSLGQSVA KATGRKYVRM ALGGVRDEAE IRGHRRTYIG SMPGKIIQKM AKVGVRNPLF
LLDEIDKMAS DFRGDPAAAL LEVLDPEQNG AFSDHYLEVD YDLSDVMFFA TSNSLNIPPA
LLDRMEVIRL SGYTEDEKLN IAKQHLVPKQ VSRNGLKPSE VLIEDSAIIG IIRYYTREAG
VRSLEREISK LCRKAVKQIL LSKGLKQVVI NDANLEEFLG VHRFDYGKAE DSNRIGQVTG
LAWTEVGGDL LTIEAAAVVG KGKLTYTGSL GDVMKESIQA AMTVVRSRAE GLRINEDFYE
KRDIHVHVPE GATPKDGPSA GIAMVTALVS SLTGNPVRAD VAMTGEITLR GEVLPIGGLK
EKLLAAHRGG IKRVLIPHDN IRDLKEIPEN VKTALEIRPV KWIEEVLEAA LQEPLARVTV
ANTVKNAAKS KKTEKNPV
//
