ID   LON_MYCAP               Reviewed;         996 AA.
AC   A5IYF2;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Lon protease;
DE            EC=3.4.21.53;
DE   AltName: Full=ATP-dependent protease La;
GN   Name=lon; OrderedLocusNames=MAG3630;
OS   Mycoplasmopsis agalactiae (strain NCTC 10123 / CIP 59.7 / PG2) (Mycoplasma
OS   agalactiae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=347257;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10123 / CIP 59.7 / PG2;
RX   PubMed=17511520; DOI=10.1371/journal.pgen.0030075;
RA   Sirand-Pugnet P., Lartigue C., Marenda M., Jacob D., Barre A., Barbe V.,
RA   Schenowitz C., Mangenot S., Couloux A., Segurens B., de Daruvar A.,
RA   Blanchard A., Citti C.;
RT   "Being pathogenic, plastic, and sexual while living with a nearly minimal
RT   bacterial genome.";
RL   PLoS Genet. 3:744-758(2007).
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; CU179680; CAL59061.1; -; Genomic_DNA.
DR   RefSeq; WP_011949536.1; NC_009497.1.
DR   AlphaFoldDB; A5IYF2; -.
DR   SMR; A5IYF2; -.
DR   STRING; 347257.MAG3630; -.
DR   EnsemblBacteria; CAL59061; CAL59061; MAG3630.
DR   KEGG; maa:MAG3630; -.
DR   HOGENOM; CLU_004109_5_0_14; -.
DR   OMA; YIEHEYD; -.
DR   Proteomes; UP000007065; 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   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..996
FT                   /note="Lon protease"
FT                   /id="PRO_0000396579"
FT   DOMAIN          797..979
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        885
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        928
FT                   /evidence="ECO:0000250"
FT   BINDING         560..567
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   996 AA;  113743 MW;  C11AF6DBC6A27556 CRC64;
     MLFDREVAKL EITDELITQT TYWKQIIDEY TKDNSNGAEI INKARIMLVY YRPAEDNRVI
     LESELQSKPT ATYADVLENV NISNLDSNMT LCQVESVEKV YDNGSQKWHY IATLKAIHKY
     ILQDIYGDEE TISSSSIDIE KLPLKYIEGM VATRFGSENN GDEMALADPS LDFNGFEEVI
     NTLIYDRNWN DAMLLYRYIR GYSAKEIRNW TKGTSEMMPD FINDDESRLE TLVRALTGFF
     LLPPYELFTI YSMPSALHQF EALKSNFVLM VRLIKKFINE LNLGNTDKLL NIYNALTDNE
     LFKNSMEQIK ENSELEVQFN YEVERIYKWH KEYLQLGYIT EDDLKLIISL IEQNQNNLSK
     RSSKKDTSAM KDKIDKELNK KIQSNLDKQQ KEFLLREKMK AIKEQLNEAD DEDGDDEYSK
     IVNDPVLKQM YPEWIIKAIK TERDKLKNMM SSSPDANITQ TYISNLKKLP WRKVEVENLD
     INRAREILDK NHYGLKEVKE RVIEYLSLII NHRNINKESS EKDLIKIDDH NQIDLQLFKE
     NTKNKAQKQF NNVPILTLVG PPGTGKTSLA RSIAEALDKS YVKLSLGGLH DESEIRGHRK
     TYVGAMPGKI IKGLQSAGVS NPLILLDEID KMSSDIKGDP TSAMLEVLDP EQNTKFQDNY
     IEHEYDLSKV LFIATANYYE NIPAPLLDRV EIIELNSYTI NEKIKIAKEH LVEVVLAQAG
     LKPDQFIIDD KALEFIIKHY TAEAGVRSLK RNLDKIARKI VTKIVSGEKI DKFVIDQNNI
     PELLGTPKIS ESEKEMQPQI GSVNGLAFTS IGGTTLQIEV SWFKSKQPGI RLTGQLKEVM
     QESAKIALSY VRANAEKFGI KNVDFDTTEI HVHVPEGAVP KDGPSAGVTF TTALISALAK
     IPVSQEVAMT GEITLRGKVL EIGGLKEKSF AAFKKGIKTV FIPKNNEKNL SDIPEEVKEA
     INFIPVSHYE QIWEHLFKGK KSDESETESK KKKQSK