ID S6G417_9MOLU Unreviewed; 776 AA.
AC S6G417;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
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:EOA07482.1};
GN ORFNames=MYEA_1320 {ECO:0000313|EMBL:EOA07482.1};
OS Mycoplasma yeatsii 13926.
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=1188240 {ECO:0000313|EMBL:EOA07482.1, ECO:0000313|Proteomes:UP000015348};
RN [1] {ECO:0000313|EMBL:EOA07482.1, ECO:0000313|Proteomes:UP000015348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13926 {ECO:0000313|EMBL:EOA07482.1,
RC ECO:0000313|Proteomes:UP000015348};
RX PubMed=23766401;
RA Dordet-Frisoni E., Baranowski E., Barre A., Blanchard A., Breton M.,
RA Couture C., Dupuy V., Gaurivaud P., Jacob D., Lemaitre C., Manso-Silvan L.,
RA Nikolski M., Nouvel L.X., Poumarat F., Sirand-Pugnet P., Thebault P.,
RA Theil S., Thiaucourt F., Citti C., Tardy F.;
RT "Draft Genome Sequences of Mycoplasma auris and Mycoplasma yeatsii, Two
RT Species of the Ear Canal of Caprinae.";
RL Genome Announc. 1:e00280-13(2013).
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:EOA07482.1}.
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DR EMBL; AORK01000007; EOA07482.1; -; Genomic_DNA.
DR RefSeq; WP_004427053.1; NZ_AORK01000007.1.
DR AlphaFoldDB; S6G417; -.
DR PATRIC; fig|1188240.3.peg.133; -.
DR eggNOG; COG0466; Bacteria.
DR OrthoDB; 9803599at2; -.
DR Proteomes; UP000015348; 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 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 6..198
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 595..776
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT COILED 185..230
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 682
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT ACT_SITE 725
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT BINDING 359..366
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 776 AA; 87995 MW; B9DFF3CA07A1607E CRC64;
MKINKIPVVV TRGIVLFPTN LKVVEFGREK SKLSIKKAEQ DFDSKVIVVS QKVPLDENPS
IDKLFEIGCL AKSSVKKVWK DGTLSTELEF ISKVKIDNFI EEDGILYAEA TVLEDQVPTT
DQEKNKIKEL ILQLGRVTSR NINEFEEAIK KDDWNNVNEL IYGLADKASF IPLPMKIKIL
ESISLEEKIN LLKDLLKDRS KAQAATGDAL SVETEINKKL KDKMDKQQKE YYLREKMRII
KEELDDEDSD RSQLDKYKKR LETEPFPENV KEKILSSIRR IETMQPGSAE VNVERNYVDW
MMSIPWWEQS EDIADLKYAQ EVLNKHHFGL KKVKERIIEY LAVKQKTKTL KGPIITLVGP
PGVGKTSLAK SIAEALGKKF VKVSLGGVKD ESEIRGHRKT YVGSMPGRVI QAMKRAKVKN
PLFLLDEIDK MASDQRGDPA SAMLEVLDPE QNKEFSDHYI EEPYDLSTVM FIATANYPEN
IPEALYDRME IINLSSYTEL EKMHIAKDYL TPKILEEDQL TEEELKFTDE AYDEMIKYYT
REAGVRQLER WISTIARKFI VKLLNGEVKN LVVDRKVVNE YLGKHIFEHT SKQDDSQVGV
VTGLAYTQFG GDILPIEVSI YPGKGNLTLT GKLGEVMKES ATIALTYVKS NYEKFGIDKD
AFKDVDIHIH VPEGAVPKDG PSAGITLTTA LISALTKKPV SKEIGMTGEI TLRGNVLPIG
GLREKSISAS RSGLKHILIP FKNQKDLDDV PKEVQDVLKI TPVSKYEEVF DIVFKK
//
