ID A0A149VYR5_9PROT Unreviewed; 813 AA.
AC A0A149VYR5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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_1 {ECO:0000313|EMBL:KXW58318.1};
GN Synonyms=lon {ECO:0000256|HAMAP-Rule:MF_01973};
GN ORFNames=FEMY_11450 {ECO:0000313|EMBL:KXW58318.1};
OS Ferrovum myxofaciens.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Ferrovales; Ferrovaceae;
OC Ferrovum.
OX NCBI_TaxID=416213 {ECO:0000313|EMBL:KXW58318.1, ECO:0000313|Proteomes:UP000075653};
RN [1] {ECO:0000313|EMBL:KXW58318.1, ECO:0000313|Proteomes:UP000075653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z-31 {ECO:0000313|EMBL:KXW58318.1,
RC ECO:0000313|Proteomes:UP000075653};
RA Poehlein A., Ullrich S.R., Schloemann M., Muehling M., Daniel R.;
RT "Genome sequence of the acidophilic iron oxidising Ferrovum strain Z-31.";
RL Submitted (JAN-2016) 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}.
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:KXW58318.1}.
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DR EMBL; LRRD01000017; KXW58318.1; -; Genomic_DNA.
DR RefSeq; WP_062187984.1; NZ_LRRD01000017.1.
DR AlphaFoldDB; A0A149VYR5; -.
DR STRING; 1789004.FEMY_11450; -.
DR PATRIC; fig|1789004.3.peg.1159; -.
DR Proteomes; UP000075653; 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; 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.
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:UP000075653};
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..203
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 813 AA; 89593 MW; 8920FA273170BC5F CRC64;
MSTVTQESVQ LPLLPLRDVV VFPHMVIPLF VGRLKSIRAL ELAMEAGKNI LLVAQKSASN
DDPGVDELYD VGSIATILQL LKLPDGTVKV LVEGVQRVTV SEVTEPNQSH FLGVATPIKE
SSSEHSELEA LRRTLLGQFE QFVKLNKKIP QEVLSSFSSI EDAGRLADTV ATHVPLKLEQ
KQEVLALFDV RKRIEQLLSL LESEIDILQV EKRIRGRVKR QMEKSQREYY LNEQVKAIQK
ELGDNEDGAD IEDLEKKIRT AHMSKEAQTK AESELKKLRL MSPMSAEATV VRNYIDTLVA
LPWKKKTRVS SDLANCEKVL DQDHFGLDKV KERIVEYLAV QARVDKVKAP ILCLVGPPGV
GKTSLGKSIA RATNRKFVRM ALGGVRDEAE IRGHRRTYIG AMPGKILQSL TKVAVRNPLF
LLDEVDKMGQ DYRGDPSSAL LEVLDPEQNH TFTDHYVEVE YDLSDVMFVA TANTLNIPSP
LLDRMEVIRL SGYTEDEKIN IARQYLLPKQ LKANGLKEDE ISVAEGALRD IVQYYTREAG
VRALDREIAK ICRKVVKYLL LSKKTGKVAV TSRNLEKYLG VRPYTFGVAE KTNQVGQVTG
LAWTEVGGEL LTIEAARVPG KGKMTTTGKL GEVMQESIQA ALSVVRSRAT RLGIHPDFYE
KSDIHIHLPE GATPKDGPSA GTAITTAMVS VLTGIPVRAD VAMTGEITLR GEVLAIGGLK
EKLLAAHRGG IRTVLIPQEN CKDLVEIPDN IKGRLELHPV RWIDQVLALA LEREPVPLPE
AGAGESIIPP VPAAATPLTP HGEVVVTPAG ITH
//
