ID   LONM_YEAST              Reviewed;        1133 AA.
AC   P36775; D6VPX8; P13435;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 2.
DT   27-MAR-2024, entry version 199.
DE   RecName: Full=Lon protease homolog, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03120};
DE            EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_03120, ECO:0000269|PubMed:35143841};
DE   Flags: Precursor;
GN   Name=PIM1 {ECO:0000255|HAMAP-Rule:MF_03120}; Synonyms=LON;
GN   OrderedLocusNames=YBL022C; ORFNames=YBL0440;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8276800; DOI=10.1016/s0021-9258(17)42340-4;
RA   van Dyck L., Pearce D.A., Sherman F.;
RT   "PIM1 encodes a mitochondrial ATP-dependent protease that is required for
RT   mitochondrial function in the yeast Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 269:238-242(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=8146662; DOI=10.1126/science.8146662;
RA   Suzuki C.K., Suda K., Wang N., Schatz G.;
RT   "Requirement for the yeast gene LON in intramitochondrial proteolysis and
RT   maintenance of respiration.";
RL   Science 264:273-276(1994).
RN   [3]
RP   ERRATUM OF PUBMED:8146662.
RX   PubMed=8178144; DOI=10.1126/science.8178144;
RA   Suzuki C.K., Suda K., Wang N., Schatz G.;
RL   Science 264:891-891(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-216.
RC   STRAIN=ATCC MYA-3516 / BWG1-7A;
RX   PubMed=2832732; DOI=10.1128/mcb.8.2.655-663.1988;
RA   Hahn S., Pinkham J., Wei R., Miller R., Guarente L.;
RT   "The HAP3 regulatory locus of Saccharomyces cerevisiae encodes divergent
RT   overlapping transcripts.";
RL   Mol. Cell. Biol. 8:655-663(1988).
RN   [7]
RP   PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, MUTAGENESIS OF LYS-638 AND
RP   SER-1015, AUTOCATALYTIC PROCESSING, AND SUBCELLULAR LOCATION.
RX   PubMed=9405361; DOI=10.1093/emboj/16.24.7317;
RA   Wagner I., van Dyck L., Savel'ev A.S., Neupert W., Langer T.;
RT   "Autocatalytic processing of the ATP-dependent PIM1 protease: crucial
RT   function of a pro-region for sorting to mitochondria.";
RL   EMBO J. 16:7317-7325(1997).
RN   [8]
RP   PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, AND SUBUNIT.
RX   PubMed=9724747; DOI=10.1073/pnas.95.18.10584;
RA   van Dijl J.M., Kutejova E., Suda K., Perecko D., Schatz G., Suzuki C.K.;
RT   "The ATPase and protease domains of yeast mitochondrial Lon: roles in
RT   proteolysis and respiration-dependent growth.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:10584-10589(1998).
RN   [9]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX   PubMed=8354406; DOI=10.1016/0014-5793(93)80190-6;
RA   Kutejova E., Durcova G., Surovkova E., Kuzela S.;
RT   "Yeast mitochondrial ATP-dependent protease: purification and comparison
RT   with the homologous rat enzyme and the bacterial ATP-dependent protease
RT   La.";
RL   FEBS Lett. 329:47-50(1993).
RN   [10]
RP   FUNCTION, AND MUTAGENESIS OF LYS-638 AND SER-1015.
RX   PubMed=8810243; DOI=10.1126/science.274.5284.103;
RA   Rep M., van Dijl J.M., Suda K., Schatz G., Grivell L.A., Suzuki C.K.;
RT   "Promotion of mitochondrial membrane complex assembly by a proteolytically
RT   inactive yeast Lon.";
RL   Science 274:103-106(1996).
RN   [11]
RP   ERRATUM OF PUBMED:8810243.
RX   DOI=10.1126/science.275.5301.737f;
RA   Rep M., van Dijl J.M., Suda K., Schatz G., Grivell L.A., Suzuki C.K.;
RL   Science 275:741-741(1997).
RN   [12]
RP   SUBUNIT.
RX   PubMed=10359790; DOI=10.1073/pnas.96.12.6787;
RA   Stahlberg H., Kutejova E., Suda K., Wolpensinger B., Lustig A., Schatz G.,
RA   Engel A., Suzuki C.K.;
RT   "Mitochondrial Lon of Saccharomyces cerevisiae is a ring-shaped protease
RT   with seven flexible subunits.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:6787-6790(1999).
RN   [13]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [14]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [15]
RP   FUNCTION.
RX   PubMed=15870080; DOI=10.1074/jbc.m502796200;
RA   Ondrovicova G., Liu T., Singh K., Tian B., Li H., Gakh O., Perecko D.,
RA   Janata J., Granot Z., Orly J., Kutejova E., Suzuki C.K.;
RT   "Cleavage site selection within a folded substrate by the ATP-dependent lon
RT   protease.";
RL   J. Biol. Chem. 280:25103-25110(2005).
RN   [16]
RP   FUNCTION, AND SUBSTRATE.
RX   PubMed=16428434; DOI=10.1128/mcb.26.3.762-776.2006;
RA   Major T., von Janowsky B., Ruppert T., Mogk A., Voos W.;
RT   "Proteomic analysis of mitochondrial protein turnover: identification of
RT   novel substrate proteins of the matrix protease pim1.";
RL   Mol. Cell. Biol. 26:762-776(2006).
RN   [17]
RP   SUBSTRATE.
RX   PubMed=20150421; DOI=10.1074/jbc.m109.065425;
RA   Bayot A., Gareil M., Rogowska-Wrzesinska A., Roepstorff P., Friguet B.,
RA   Bulteau A.L.;
RT   "Identification of novel oxidized protein substrates and physiological
RT   partners of the mitochondrial ATP-dependent Lon-like protease Pim1.";
RL   J. Biol. Chem. 285:11445-11457(2010).
RN   [18]
RP   SUBSTRATE.
RX   PubMed=28377575; DOI=10.1038/s41598-017-00632-8;
RA   Kunova N., Ondrovicova G., Bauer J.A., Bellova J., Ambro L.,
RA   Martinakova L., Kotrasova V., Kutejova E., Pevala V.;
RT   "The role of Lon-mediated proteolysis in the dynamics of mitochondrial
RT   nucleic acid-protein complexes.";
RL   Sci. Rep. 7:631-631(2017).
RN   [19] {ECO:0007744|PDB:7SXO}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF 182-1133 IN COMPLEX
RP   WITH ADP; ATP AND SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP   MUTAGENESIS OF SER-1015.
RX   PubMed=35143841; DOI=10.1016/j.jbc.2022.101694;
RA   Yang J., Song A.S., Wiseman R.L., Lander G.C.;
RT   "Cryo-EM structure of hexameric yeast Lon protease (PIM1) highlights the
RT   importance of conserved structural elements.";
RL   J. Biol. Chem. 298:101694-101694(2022).
CC   -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC       degradation of misfolded, unassembled or oxidatively damaged
CC       polypeptides as well as certain short-lived regulatory proteins in the
CC       mitochondrial matrix. May also have a chaperone function in the
CC       assembly of inner membrane protein complexes. Participates in the
CC       regulation of mitochondrial gene expression and in the maintenance of
CC       the integrity of the mitochondrial genome. Binds to mitochondrial DNA
CC       in a site-specific manner (PubMed:15870080, PubMed:16428434,
CC       PubMed:8146662, PubMed:8276800, PubMed:8354406, PubMed:8810243,
CC       PubMed:9405361, PubMed:9724747, PubMed:35143841). Endogenous substrates
CC       include ABF2, ACO2, ILV1, ILV2, LSC1, LYS4, MGM101 and several oxidized
CC       proteins. The 2 nucleic acid-binding proteins ABF2 and MGM101 are
CC       protected from degradation by PIM1 when they are bound to DNA
CC       (PubMed:16428434, PubMed:20150421, PubMed:28377575).
CC       {ECO:0000255|HAMAP-Rule:MF_03120, ECO:0000269|PubMed:15870080,
CC       ECO:0000269|PubMed:16428434, ECO:0000269|PubMed:20150421,
CC       ECO:0000269|PubMed:28377575, ECO:0000269|PubMed:35143841,
CC       ECO:0000269|PubMed:8146662, ECO:0000269|PubMed:8276800,
CC       ECO:0000269|PubMed:8354406, ECO:0000269|PubMed:8810243,
CC       ECO:0000269|PubMed:9405361, ECO:0000269|PubMed:9724747}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03120,
CC         ECO:0000269|PubMed:35143841};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=40 uM for ATP for ATPase activity {ECO:0000269|PubMed:8354406};
CC       pH dependence:
CC         Optimum pH is 7.9. {ECO:0000269|PubMed:8354406};
CC   -!- SUBUNIT: Homohexamer (PubMed:35143841) (Probable). Organized in a ring
CC       with a central cavity (PubMed:10359790). The ATP-binding and
CC       proteolytic domains (AP-domain) form a hexameric chamber
CC       (PubMed:35143841). Oligomerization is independent of its proteolytic
CC       activity and the autocatalytic maturation of its subunits
CC       (PubMed:9724747). {ECO:0000255|HAMAP-Rule:MF_03120,
CC       ECO:0000269|PubMed:10359790, ECO:0000269|PubMed:35143841,
CC       ECO:0000269|PubMed:9724747, ECO:0000305|PubMed:8354406,
CC       ECO:0000305|PubMed:9724747}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC       Rule:MF_03120, ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:9405361}.
CC   -!- MISCELLANEOUS: Present with 14500 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03120}.
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DR   EMBL; X74544; CAA52634.1; -; Genomic_DNA.
DR   EMBL; L28110; AAA53625.1; -; mRNA.
DR   EMBL; Z35783; CAA84841.1; -; Genomic_DNA.
DR   EMBL; M20318; AAA53539.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07098.1; -; Genomic_DNA.
DR   PIR; S43938; S43938.
DR   RefSeq; NP_009531.1; NM_001178262.1.
DR   PDB; 7SXO; EM; 3.30 A; A/B/C/D/E/F=182-1133.
DR   PDBsum; 7SXO; -.
DR   AlphaFoldDB; P36775; -.
DR   EMDB; EMD-25502; -.
DR   SMR; P36775; -.
DR   BioGRID; 32676; 136.
DR   DIP; DIP-6629N; -.
DR   IntAct; P36775; 16.
DR   STRING; 4932.YBL022C; -.
DR   MEROPS; S16.010; -.
DR   iPTMnet; P36775; -.
DR   MaxQB; P36775; -.
DR   PaxDb; 4932-YBL022C; -.
DR   PeptideAtlas; P36775; -.
DR   EnsemblFungi; YBL022C_mRNA; YBL022C; YBL022C.
DR   GeneID; 852259; -.
DR   KEGG; sce:YBL022C; -.
DR   AGR; SGD:S000000118; -.
DR   SGD; S000000118; PIM1.
DR   VEuPathDB; FungiDB:YBL022C; -.
DR   eggNOG; KOG2004; Eukaryota.
DR   GeneTree; ENSGT00530000063553; -.
DR   HOGENOM; CLU_004109_1_0_1; -.
DR   InParanoid; P36775; -.
DR   OMA; YVGPPIY; -.
DR   OrthoDB; 1103874at2759; -.
DR   BioCyc; YEAST:G3O-28925-MONOMER; -.
DR   BRENDA; 3.4.21.53; 984.
DR   BioGRID-ORCS; 852259; 6 hits in 10 CRISPR screens.
DR   PRO; PR:P36775; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P36775; Protein.
DR   GO; GO:0005759; C:mitochondrial matrix; IMP:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
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; IMP:SGD.
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:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:UniProtKB-UniRule.
DR   GO; GO:0051131; P:chaperone-mediated protein complex assembly; IGI:SGD.
DR   GO; GO:0032042; P:mitochondrial DNA metabolic process; TAS:AgBase.
DR   GO; GO:0033108; P:mitochondrial respiratory chain complex assembly; TAS:AgBase.
DR   GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR   GO; GO:0070407; P:oxidation-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; TAS:AgBase.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IMP:SGD.
DR   GO; GO:1901858; P:regulation of mitochondrial DNA metabolic process; IMP:SGD.
DR   GO; GO:0009408; P:response to heat; TAS:AgBase.
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_03120; lonm_euk; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
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; IPR027503; Lonm_euk.
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; PTHR43718; LON PROTEASE; 1.
DR   PANTHER; PTHR43718:SF2; LON PROTEASE HOMOLOG, MITOCHONDRIAL; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   Pfam; PF02190; LON_substr_bdg; 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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Direct protein sequencing; DNA-binding;
KW   Hydrolase; Mitochondrion; Nucleotide-binding; Protease; Reference proteome;
KW   Serine protease; Transit peptide.
FT   TRANSIT         1..37
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT   PROPEP          38..98
FT                   /note="Removed in mature form; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120,
FT                   ECO:0000269|PubMed:9405361, ECO:0000269|PubMed:9724747"
FT                   /id="PRO_0000395761"
FT   CHAIN           99..1133
FT                   /note="Lon protease homolog, mitochondrial"
FT                   /id="PRO_0000026733"
FT   DOMAIN          182..480
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          923..1109
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   REGION          98..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          282..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          839..892
FT                   /note="Dispensable for catalytic activity"
FT                   /evidence="ECO:0000269|PubMed:35143841"
FT   REGION          844..889
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..142
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..305
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..349
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        856..889
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1015
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT   ACT_SITE        1058
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT   BINDING         632..639
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120,
FT                   ECO:0000269|PubMed:35143841, ECO:0007744|PDB:7SXO"
FT   MUTAGEN         638
FT                   /note="K->N: Abolishes ATP-binding."
FT                   /evidence="ECO:0000269|PubMed:8810243,
FT                   ECO:0000269|PubMed:9405361"
FT   MUTAGEN         1015
FT                   /note="S->A: Abolishes peptidase activity."
FT                   /evidence="ECO:0000269|PubMed:35143841,
FT                   ECO:0000269|PubMed:8810243, ECO:0000269|PubMed:9405361"
FT   CONFLICT        509
FT                   /note="Q -> R (in Ref. 2; AAA53625)"
FT                   /evidence="ECO:0000305"
FT   HELIX           531..537
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   HELIX           541..555
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   STRAND          559..561
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   HELIX           562..576
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   HELIX           589..599
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   HELIX           604..618
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   STRAND          627..631
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   TURN            638..640
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   HELIX           641..648
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   STRAND          653..656
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   HELIX           665..668
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   HELIX           681..689
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   STRAND          691..693
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   STRAND          695..698
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   STRAND          708..710
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   HELIX           713..721
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   TURN            723..725
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   HELIX           726..728
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   STRAND          732..734
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   STRAND          743..750
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   HELIX           757..762
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   STRAND          763..767
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   HELIX           773..791
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   TURN            796..798
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   STRAND          799..801
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   HELIX           803..812
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   HELIX           820..839
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   STRAND          899..901
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   TURN            903..906
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   HELIX           907..910
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   STRAND          928..935
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   STRAND          938..949
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   STRAND          960..962
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   HELIX           967..988
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   HELIX           994..996
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   STRAND          1000..1003
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   HELIX           1017..1029
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   STRAND          1037..1039
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   STRAND          1041..1043
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   STRAND          1048..1050
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   HELIX           1055..1064
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   STRAND          1068..1073
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   HELIX           1074..1076
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   HELIX           1077..1082
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   HELIX           1085..1088
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   STRAND          1092..1098
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   HELIX           1099..1106
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   TURN            1112..1114
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   STRAND          1115..1119
FT                   /evidence="ECO:0007829|PDB:7SXO"
FT   HELIX           1120..1128
FT                   /evidence="ECO:0007829|PDB:7SXO"
SQ   SEQUENCE   1133 AA;  127112 MW;  281CAB94579FFF09 CRC64;
     MLRTRTTKTL STVARTTRAI QYYRSIAKTA AVSQRRFAST LTVRDVENIK PSHIIKSPTW
     QEFQHQLKDP RYMEHFAQLD AQFARHFMAT NSGKSILAKD DSTSQKKDED VKIVPDEKDT
     DNDVEPTRDD EIVNKDQEGE ASKNSRSSAS GGGQSSSSRS DSGDGSSKQK PPKDVPEVYP
     QMLALPIARR PLFPGFYKAV VISDERVMKA IKEMLDRQQP YIGAFMLKNS EEDTDVITDK
     NDVYDVGVLA QITSAFPSKD EKTGTETMTA LLYPHRRIKI DELFPPNEEK EKSKEQAKDT
     DTETTVVEDA NNPEDQESTS PATPKLEDIV VERIPDSELQ HHKRVEATEE ESEELDDIQE
     GEDINPTEFL KNYNVSLVNV LNLEDEPFDR KSPVINALTS EILKVFKEIS QLNTMFREQI
     ATFSASIQSA TTNIFEEPAR LADFAAAVSA GEEDELQDIL SSLNIEHRLE KSLLVLKKEL
     MNAELQNKIS KDVETKIQKR QREYYLMEQL KGIKRELGID DGRDKLIDTY KERIKSLKLP
     DSVQKIFDDE ITKLSTLETS MSEFGVIRNY LDWLTSIPWG KHSKEQYSIP RAKKILDEDH
     YGMVDVKDRI LEFIAVGKLL GKVDGKIICF VGPPGVGKTS IGKSIARALN RKFFRFSVGG
     MTDVAEIKGH RRTYIGALPG RVVQALKKCQ TQNPLILIDE IDKIGHGGIH GDPSAALLEV
     LDPEQNNSFL DNYLDIPIDL SKVLFVCTAN SLETIPRPLL DRMEVIELTG YVAEDKVKIA
     EQYLVPSAKK SAGLENSHVD MTEDAITALM KYYCRESGVR NLKKHIEKIY RKAALQVVKK
     LSIEDSPTSS ADSKPKESVS SEEKAENNAK SSSEKTKDNN SEKTSDDIEA LKTSEKINVS
     ISQKNLKDYV GPPVYTTDRL YETTPPGVVM GLAWTNMGGC SLYVESVLEQ PLHNCKHPTF
     ERTGQLGDVM KESSRLAYSF AKMYLAQKFP ENRFFEKASI HLHCPEGATP KDGPSAGVTM
     ATSFLSLALN KSIDPTVAMT GELTLTGKVL RIGGLREKAV AAKRSGAKTI IFPKDNLNDW
     EELPDNVKEG LEPLAADWYN DIFQKLFKDV NTKEGNSVWK AEFEILDAKK EKD
//