ID A0A0H3XHZ5_9MOLU Unreviewed; 779 AA.
AC A0A0H3XHZ5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=lonA {ECO:0000313|EMBL:AKM54050.1};
GN Synonyms=lon {ECO:0000256|HAMAP-Rule:MF_01973};
GN ORFNames=SERIO_v1c04710 {ECO:0000313|EMBL:AKM54050.1};
OS Spiroplasma eriocheiris.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=315358 {ECO:0000313|EMBL:AKM54050.1, ECO:0000313|Proteomes:UP000035661};
RN [1] {ECO:0000313|EMBL:AKM54050.1, ECO:0000313|Proteomes:UP000035661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TDA-040725-5 {ECO:0000313|Proteomes:UP000035661};
RX PubMed=26254485; DOI=10.1093/gbe/evv160;
RA Lo W.S., Gasparich G.E., Kuo C.H.;
RT "Found and Lost: The Fates of Horizontally Acquired Genes in Arthropod-
RT Symbiotic Spiroplasma.";
RL Genome Biol. Evol. 7:2458-2472(2015).
RN [2] {ECO:0000313|Proteomes:UP000035661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TDA-040725-5 {ECO:0000313|Proteomes:UP000035661};
RA Lo W.-S., Kuo C.-H.;
RT "Complete genome sequence of Spiroplasma eriocheiris TDA-040725-5 (DSM
RT 21848).";
RL Submitted (JUN-2015) 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}.
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DR EMBL; CP011856; AKM54050.1; -; Genomic_DNA.
DR RefSeq; WP_047791296.1; NZ_CP011856.1.
DR AlphaFoldDB; A0A0H3XHZ5; -.
DR STRING; 315358.SERIO_v1c04710; -.
DR KEGG; seri:SERIO_v1c04710; -.
DR PATRIC; fig|743698.3.peg.472; -.
DR Proteomes; UP000035661; Chromosome.
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:UP000035661};
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 17..206
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 596..777
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 683
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT ACT_SITE 726
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT BINDING 360..367
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 779 AA; 88155 MW; FA847758230D4A54 CRC64;
MAEPINQSTE TTQLKNVPVL VTRGSYIFPG FEQVLEVGRD KSILAVNTAN KEFDNHIVLV
SQKKPLEDDP KLSGIYRIGV LAELKIRKVW EDGSLTVNFK AVDRVKLLDL REGEYYTADI
DILKSVIKSE DKIVEKITSN IKQLMELQDI LPEDLLEQIG DSVDGNEVVD TIAQFLPFIP
VAKKQDILEE LDVEKRLQII FDHLVNKQQV SDIDNKISKK IKERVDEQQR EYYLREKLKA
IKDELGEFDD AADEMKVYKE RLEKEPFPKN IKERIEQEIA RYESLPQASS ESNIIRTYID
WMMQIPWWER TEEKNDLKYA KEMLDKYHFG LDKVKERIIE YLAVKTMTNS LKGQIICLVG
PPGVGKTSLA KSIAEATGRN FVKVALGGVK DESEIRGHRK TYIGAMPGRI IQSMKRAKTI
NPLFLLDEID KMSSDYRGDP ASAMLEVLDP EQNATFSDHY IEENYDLGNV MFIATANYYD
NIPEALIDRM EIIQLSSYTE LEKFHIAKDY LVPKVLTNNG LADVQLIFAD DAINEIIKHY
TREAGVRQLE RDLNAVARKF IVKFLNKEMT NLTVTPQVVN ELLGKRRFEH TEAEKESQIG
VVTGLAYTQF GGDILPIEVN TFPGKGNFVL TGKLGDVMKE SASIALDYVK ANAEKYSIDP
KFFETHDVHI HVPEGAVPKD GPSAGITLTT AIISALSNRP VSKDIGMTGE ITLRGQVLPI
GGLREKSISA KRSGLKTILI PNKNLKDLDD IPKEVQDTLK IIPVATYDEV FKNVFGKLD
//
