ID A0A1A7QAJ3_9PAST Unreviewed; 800 AA.
AC A0A1A7QAJ3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=QS62_03855 {ECO:0000313|EMBL:OBW95264.1}, QV08_03470
GN {ECO:0000313|EMBL:OBX08772.1};
OS Gallibacterium salpingitidis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Gallibacterium.
OX NCBI_TaxID=505341 {ECO:0000313|EMBL:OBX08772.1, ECO:0000313|Proteomes:UP000092603};
RN [1] {ECO:0000313|Proteomes:UP000092603, ECO:0000313|Proteomes:UP000092649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=19987/2 Salp {ECO:0000313|EMBL:OBX08772.1,
RC ECO:0000313|Proteomes:UP000092603}, and F150
RC {ECO:0000313|EMBL:OBW95264.1, ECO:0000313|Proteomes:UP000092649};
RA Kudirkiene E., Bojesen A.M.;
RT "Pan-genome of Gallibacterium spp.";
RL Submitted (NOV-2014) 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: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:OBX08772.1}.
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DR EMBL; JTJL01000013; OBW95264.1; -; Genomic_DNA.
DR EMBL; JTJT01000017; OBX08772.1; -; Genomic_DNA.
DR RefSeq; WP_066106208.1; NZ_JTJU01000017.1.
DR AlphaFoldDB; A0A1A7QAJ3; -.
DR STRING; 505341.QV08_03470; -.
DR PATRIC; fig|505341.3.peg.779; -.
DR OrthoDB; 9803599at2; -.
DR Proteomes; UP000092603; Unassembled WGS sequence.
DR Proteomes; UP000092649; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
KW DNA-binding {ECO:0000313|EMBL:OBX08772.1};
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:UP000092649};
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 COILED 230..257
FT /evidence="ECO:0000256|SAM:Coils"
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 800 AA; 89277 MW; 46D7E58D5CFFD1AF CRC64;
MNKELSDTKQ IPVLPLRDVV VFPHIVMPLY VGRAKSIRSL DEAMESGRDV LLVTQKEANL
EEPRAEDIYQ VGTIATILQL LKLPDGTVKV LVEGKSRAKI EHFADDEYFS ALVTEIPEII
DNQQELNVIQ NTVLTELDKF STQQHNKMKP EVLAALKDID APEKLSDTLA GNMPLSIEKK
QSLLEEADVL KRFEALIGLI QTEMEINSID KKIRDRVKKQ MEKNQRDYYL NEQIKAIQKE
LGEVEGVENE IQQLKKKIAD AKMPKAVEEK AEAELQKLKM MSPMSAEATV VRSYIDWMVQ
VPWHKRTKVK KDLKQAEEVL NNDHYGLERV KERILEYLAV QTRTNQMRGP ILCLVGPPGV
GKTSLGQSIA QATGRKYVRM ALGGVRDEAE IRGHRRTYIG ALPGKLIQNM AKVGVKNPLF
LLDEIDKLGA DMRGDPASAL LEVLDPEQNN TFSDHYLEVD YDLSDVMFVA TSNSMNIPGP
LLDRMEVIRL SGYTEDEKLN IATRHLLKKQ IERNGLKEKE LVLKEEAILD IIRYYTREAG
VRSLEREISK ICRKAVKNLL LDKSLKQVVV DSSNLHDYLG VRRFEYGKAD NQNRIGEVTG
LAWTEVGGDL LTIESASVSG KGKLNYTGSL GDVMKESIQA AMTVVRARAE QLGISPDFYE
KRDIHIHVPE GATPKDGPSA GIAMCTALVS CLTGNPVRAD VAMTGEITLR GKVLPIGGLK
EKLLAAHRGG IKRVLIPKDN VKDLEEIPEN AKAALDIRPV ETIDEVLALA LEKPPVGIEV
IKDLAKPKKR TTKSVTSTVN
//
