ID A0AAJ2NNU9_ALKPS Unreviewed; 775 AA. AC A0AAJ2NNU9; DT 24-JUL-2024, integrated into UniProtKB/TrEMBL. DT 24-JUL-2024, sequence version 1. DT 02-OCT-2024, entry version 2. 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 ECO:0000313|EMBL:MDV2885829.1}; GN ORFNames=RYX45_11620 {ECO:0000313|EMBL:MDV2885829.1}; OS Alkalihalophilus pseudofirmus (Bacillus pseudofirmus). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalihalophilus. OX NCBI_TaxID=79885 {ECO:0000313|EMBL:MDV2885829.1, ECO:0000313|Proteomes:UP001285636}; RN [1] {ECO:0000313|EMBL:MDV2885829.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BZ-TG-HK211 {ECO:0000313|EMBL:MDV2885829.1}; RA Zhao B., Guo T.; RT "Screening of Alkalihalophilus pseudofirmusBZ-TG-HK211 and Its Alleviation RT of Salt Stress on Rapeseed Growth."; RL Submitted (OCT-2023) 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:MDV2885829.1}. 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; JAWJAY010000002; MDV2885829.1; -; Genomic_DNA. DR Proteomes; UP001285636; Unassembled WGS sequence. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. 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; PF22667; Lon_lid; 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 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 10..204 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|PROSITE-ProRule:PRU01122" FT ACT_SITE 722 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973, FT ECO:0000256|PROSITE-ProRule:PRU01122" FT BINDING 356..363 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973" SQ SEQUENCE 775 AA; 87270 MW; F4B191703D15057A CRC64; MVAEKKKRRI PLLPLRGLLV FPSMVLHLDV GRAKSVQALE FAMNEDEEIL LSTQKEISID EPTEDEIYSI GTIAKIKQLL KLPNGTVRIH VEGLYRAEIE QYVENAEFLE VDISPLTEEQ KERTTETQAI MRSLLEMFEQ YTKVSKKVSQ ETLATVSDIT EPHRFADVLA SNLPLKLAEK QELLEMNNVV ERLLHLIDIL NNEQEVLGLE KKIGQRVKKS MEKTQKEYYL REQMKAIQKE LGDREGRGGE VATLREKIEE AEMPESVEEK ALKELDRYEK MPANSAESSV LRNYIEWLIQ LPWVYETEDQ LDVNRAEEIL NEDHYGLEKV KERVLEYLAV QQLTNELKGP ILCLSGPPGV GKTSLARSIA RSLDREFVRI SLGGVRDEAE IRGHRRTYVG AMPGRMIQGM KKAGSINPVF LLDEIDKMAN DFRGDPSSAL LEVLDPEQNH NFSDHYIEEP YDLSKVMFVT TANNIATIPG PLRDRMEMIH IAGYTEVEKM QIAKNYLLPK QMKDHGIKKS MMQVKDEAIQ KVIRYYTREA GVRNLERQLA TLCRKAAKMI VTGTKKRVIL TAKTVEDMLG KPRFRYGQAE EEDQVGAATG LAYTSAGGDT LSIEVSLAPG KGKLTLTGKL GDVMKESAQA AFSYIRARSK ELEIEPDFHE KNDIHIHVPE GATPKDGPSA GITMATALIS ALTGRVVKKE VGMTGEITLR GRVLPIGGLK EKSMSAHRAG LKTIIIPKDN EKDLEDVPES VREDLNYILV GHLDDVLKHA LGEKK //