LON_MYCMO
ID LON_MYCMO Reviewed; 833 AA.
AC Q6KI22;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Lon protease {ECO:0000255|HAMAP-Rule:MF_01973};
DE EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_01973};
DE AltName: Full=ATP-dependent protease La {ECO:0000255|HAMAP-Rule:MF_01973};
GN Name=lon {ECO:0000255|HAMAP-Rule:MF_01973}; OrderedLocusNames=MMOB2680;
OS Mycoplasma mobile (strain ATCC 43663 / 163K / NCTC 11711) (Mesomycoplasma
OS mobile).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX NCBI_TaxID=267748;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43663 / 163K / NCTC 11711;
RX PubMed=15289470; DOI=10.1101/gr.2674004;
RA Jaffe J.D., Stange-Thomann N., Smith C., DeCaprio D., Fisher S., Butler J.,
RA Calvo S., Elkins T., FitzGerald M.G., Hafez N., Kodira C.D., Major J.,
RA Wang S., Wilkinson J., Nicol R., Nusbaum C., Birren B., Berg H.C.,
RA Church G.M.;
RT "The complete genome and proteome of Mycoplasma mobile.";
RL Genome Res. 14:1447-1461(2004).
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:0000255|HAMAP-Rule:MF_01973}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01973};
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- INDUCTION: By heat shock. {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_01973}.
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DR EMBL; AE017308; AAT27754.1; -; Genomic_DNA.
DR RefSeq; WP_011264788.1; NC_006908.1.
DR AlphaFoldDB; Q6KI22; -.
DR SMR; Q6KI22; -.
DR STRING; 267748.MMOB2680; -.
DR MEROPS; S16.001; -.
DR EnsemblBacteria; AAT27754; AAT27754; MMOB2680.
DR KEGG; mmo:MMOB2680; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_14; -.
DR OMA; KKMNPVM; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000009072; 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 Gene3D; 2.30.130.40; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR015947; PUA-like_sf.
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 Pfam; PF02190; LON_substr_bdg; 1.
DR PIRSF; PIRSF001174; Lon_proteas; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00763; lon; 1.
DR PROSITE; PS51787; LON_N; 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..833
FT /note="Lon protease"
FT /id="PRO_0000396582"
FT DOMAIN 3..196
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 627..808
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 714
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 757
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 390..397
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 833 AA; 94358 MW; A282DD34C82DE936 CRC64;
MKYPFMATRG VITFIGNSST IEVGRPLSLA AIDLAKSDFE NKLVLIPQKN IKQNEIEFEK
DLENVGILTK IKSIKILSNG NRKIIVEGVE RIKLDSIEKD KNNNDIIANL SLYPVLKNEN
GSSETIIEKM QTSLNNIIES NLPLVANQEL SKHESSERYT YILAHYLTMP FEKKFEIFAK
KSLTEMLELI FSFLVELKNI QKLDVDLDKD IKKNLDSQQR EYLLRERLKV IQKKLGDDEN
DEEEIEEKLN SKYGKEQYPE EVIKTIKNEK RRLKNMMSSS PEANTSRTYI EWLTNLPWRK
VSVDKTNLVK SKEILDSYHY GLKEVKERII EFLAVMINNN KKHPEDEKTK IQIPNSDYEI
NKNLFTKKNA SDDTYSYKSS NNVPILALVG PPGTGKTSLA KAIAETLDRK FIKISLGGVK
DEAEIRGHRR TYVGALPGKI IQAIKKAGVS NPVILLDEID KMSSDYKGDP TSAMLEVLDP
EQNVNFQDHY IELEYDLSKV LFIATANYYQ NISAPLLDRV EIIELSSYTS LEKIRIARDY
LIKKVLEQNS LEESQFKISD ESLDFLIKHY TLEAGVRNLQ RALDKLARKI VVKSLENKLE
KDFVITSEEI VNLLGVIKYT DDFKENYERI GAVNGLAYTQ YGGSTLSIEV TTFPNSKGGI
KLTGQLKEVM QESAQIALAF VRSNAKKYEI DFNFEANQIH IHVPEGAVPK DGPSAGVTFT
TAIISALKQI PVSHKVGMTG EITLRGKVLP IGGLKEKSLA AHKLGIKTVF IPNENNRNLV
EVADEVKESI EFISVSDYDE IFENLFGKLS DNKKITSNSK IPKKDISKAN PTH
