ID   LON_MYCS5               Reviewed;         890 AA.
AC   Q4A696;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Lon protease;
DE            EC=3.4.21.53;
DE   AltName: Full=ATP-dependent protease La;
GN   Name=lon; OrderedLocusNames=MS53_0312;
OS   Mycoplasmopsis synoviae (strain 53) (Mycoplasma synoviae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=262723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=53;
RX   PubMed=16077101; DOI=10.1128/jb.187.16.5568-5577.2005;
RA   Vasconcelos A.T.R., Ferreira H.B., Bizarro C.V., Bonatto S.L.,
RA   Carvalho M.O., Pinto P.M., Almeida D.F., Almeida L.G.P., Almeida R.,
RA   Alves-Junior L., Assuncao E.N., Azevedo V.A.C., Bogo M.R., Brigido M.M.,
RA   Brocchi M., Burity H.A., Camargo A.A., Camargo S.S., Carepo M.S.,
RA   Carraro D.M., de Mattos Cascardo J.C., Castro L.A., Cavalcanti G.,
RA   Chemale G., Collevatti R.G., Cunha C.W., Dallagiovanna B., Dambros B.P.,
RA   Dellagostin O.A., Falcao C., Fantinatti-Garboggini F., Felipe M.S.S.,
RA   Fiorentin L., Franco G.R., Freitas N.S.A., Frias D., Grangeiro T.B.,
RA   Grisard E.C., Guimaraes C.T., Hungria M., Jardim S.N., Krieger M.A.,
RA   Laurino J.P., Lima L.F.A., Lopes M.I., Loreto E.L.S., Madeira H.M.F.,
RA   Manfio G.P., Maranhao A.Q., Martinkovics C.T., Medeiros S.R.B.,
RA   Moreira M.A.M., Neiva M., Ramalho-Neto C.E., Nicolas M.F., Oliveira S.C.,
RA   Paixao R.F.C., Pedrosa F.O., Pena S.D.J., Pereira M., Pereira-Ferrari L.,
RA   Piffer I., Pinto L.S., Potrich D.P., Salim A.C.M., Santos F.R., Schmitt R.,
RA   Schneider M.P.C., Schrank A., Schrank I.S., Schuck A.F., Seuanez H.N.,
RA   Silva D.W., Silva R., Silva S.C., Soares C.M.A., Souza K.R.L., Souza R.C.,
RA   Staats C.C., Steffens M.B.R., Teixeira S.M.R., Urmenyi T.P.,
RA   Vainstein M.H., Zuccherato L.W., Simpson A.J.G., Zaha A.;
RT   "Swine and poultry pathogens: the complete genome sequences of two strains
RT   of Mycoplasma hyopneumoniae and a strain of Mycoplasma synoviae.";
RL   J. Bacteriol. 187:5568-5577(2005).
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 (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC   -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: By heat shock. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01122}.
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DR   EMBL; AE017245; AAZ43725.1; -; Genomic_DNA.
DR   RefSeq; WP_011283457.1; NC_007294.1.
DR   AlphaFoldDB; Q4A696; -.
DR   SMR; Q4A696; -.
DR   STRING; 262723.MS53_0312; -.
DR   EnsemblBacteria; AAZ43725; AAZ43725; MS53_0312.
DR   KEGG; msy:MS53_0312; -.
DR   eggNOG; COG0466; Bacteria.
DR   HOGENOM; CLU_004109_5_2_14; -.
DR   OMA; GAWQVVD; -.
DR   Proteomes; UP000000549; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   PANTHER; PTHR10046; PTHR10046; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   PIRSF; PIRSF001174; Lon_proteas; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   TIGRFAMs; TIGR00763; lon; 1.
DR   PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW   Reference proteome; Serine protease; Stress response.
FT   CHAIN           1..890
FT                   /note="Lon protease"
FT                   /id="PRO_0000396585"
FT   DOMAIN          698..880
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        786
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        829
FT                   /evidence="ECO:0000250"
FT   BINDING         461..468
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   890 AA;  102244 MW;  16CDC6C6DAA5AABB CRC64;
     MQKKQTLNYV IVKTDEISFP FGYSEVLILE QDSIELLETT KFKFKNEDRL VIVYAEDVYT
     EEVKFLQRGL YIKPLDAKEV MYQGEKALIL TFKALHFFDI QNFSYEMNQD EIMSANFLVD
     GNAKGTVGYE MVLSGHINNV EDVKENLMNE FRQDQNKMNF FSIFETLVNN SNSFGISTNN
     QAGTAMLFKQ NYGAKDEVKP YDIEEIKALI DSKITQDNDP SEFLLNNFES LMTYFGFLDL
     NKFPHKWHLY NSFDYGNFTR LINEVGNFIQ TALKLEENIT SEISKKLNNQ QKEFMLREKR
     KVIDDELAKL GKDTLQDDKD EYVKKLKNKT LKKMYPDSIK EIIRDETKRY SEMMQASPEA
     NLVKNYVEYL KKLPWRKVSK DRLDIKYARE VLEKYHYGIK EVKERILEHL GVLINAQTYN
     KNYKNEVVSI DENYEIDLNL FKDKPSEKTV FNNVPILALV GPPGTGKTTL AKAISEALNK
     KYVKISLGGV KDESEIRGHR RTYVGAMPGK IVKGVAKAGV SNAVFLLDEI DKMASDHKGD
     PASAMLEVLD PEQNAQFQDH YLEQEYDLSK IIFIATANYF QNIPEALIDR VEVIELDPYT
     LNEKVQIAQK HLIPKVINEV YLDEKLFNIP EETLRFIINR YTREAGVRGL KRILDKIARK
     IVIKRVLEPD LKSFDISLNN LEELLGVAPY KTDEDKHDEI PGIATGLAYS THGGSDLEIE
     VNVFKSEKGG IQLTGSLKDV MKESAQIALT YVRSNAKYFG IHSFDFDKHT IHIHVPEGAT
     PKDGPSAGVT FTTAIISALT RLPVPNNYAM TGEITLQGKV LPIGGLKEKS FAAYWKKIKY
     VFIPHANIDN LQKIPDEIKR EITYIPVKRY DEIFQILFRD QKPENTITFN