LON2_MYXXA
ID LON2_MYXXA Reviewed; 827 AA.
AC P36774;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Lon protease 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01973};
GN Name=lon2 {ECO:0000255|HAMAP-Rule:MF_01973}; Synonyms=bsgA, lonD;
OS Myxococcus xanthus.
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Myxococcaceae; Myxococcus.
OX NCBI_TaxID=34;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DZF1;
RX PubMed=8331083; DOI=10.1128/jb.175.14.4545-4549.1993;
RA Tojo N., Inouye S., Komano T.;
RT "The lonD gene is homologous to the lon gene encoding an ATP-dependent
RT protease and is essential for the development of Myxococcus xanthus.";
RL J. Bacteriol. 175:4545-4549(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-10.
RC STRAIN=M102;
RX PubMed=8331082; DOI=10.1128/jb.175.14.4538-4544.1993;
RA Gill R.E., Karlok M., Benton D.;
RT "Myxococcus xanthus encodes an ATP-dependent protease which is required for
RT developmental gene transcription and intercellular signaling.";
RL J. Bacteriol. 175:4538-4544(1993).
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.
CC -!- DEVELOPMENTAL STAGE: Expressed during both vegetative growth and
CC development.
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; D13204; BAA02491.1; -; Genomic_DNA.
DR EMBL; L19301; AAA72018.1; -; Unassigned_DNA.
DR PIR; A36895; A36895.
DR RefSeq; WP_011554003.1; NZ_JABFNQ010000003.1.
DR AlphaFoldDB; P36774; -.
DR SMR; P36774; -.
DR GeneID; 41361325; -.
DR OMA; MVNIEDK; -.
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; IPR008268; Peptidase_S16_AS.
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.
DR PROSITE; PS01046; LON_SER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Nucleotide-binding; Protease; Serine protease; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8331082"
FT CHAIN 2..827
FT /note="Lon protease 2"
FT /id="PRO_0000076143"
FT DOMAIN 33..225
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 615..796
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 702
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 745
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 379..386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 827 AA; 90438 MW; 558E918A4A965126 CRC64;
MSDEKKKGSA ASAMPTAMAP PGLINKEDIP QVLPILPLRN SVFFPGGVLP LAVGRQKTIA
LIKDAVRDDQ VIGVVTQRRA EEEDPGAADL YTMGTVARIV KLLKMGEDNY SLVVQGLARF
RVVELVQEAP YLKARVDAVE DKTSSENVEV EALGINLKKL AREVIELMPE LPAAATELVE
SITHPGHLAD LIAANVDVPI EEKQAVLETV DLKARMKLVL ELLNRKREIL KLSNKIDSAV
KGEMSKTQRE YYLRQQLKAI KEELGEMGEE EEELDELQER LKKAGLPPDV EKVANKELNR
LKTIPAASSE YTVARTYLDW IADLPWAKIS EDNLDIENAR QQLDKDHFGI KKVKKRILEY
LAVRKLKNDM RGPILCLVGP PGVGKTSLGQ SVAKATGRKF VRLSLGGVRD EAEIRGHRRT
YVGALPGRFI QSMKKAGTKN PVMMLDEIDK LGADFRGDPS AALLEVLDPE QNNTFSDHYL
DVPFDLSKVM FVATANQLDP IPGPLRDRME IIELTGYTFE EKQSIARIHL VPKQLKEHGL
SPDHIDITDE ALLTLTTAYT REAGVRNLER RIADICRAVA VEVAGGKTEK QTINADRVKE
ILGPEMFYSE VAERTEVPGV ATGLAWTAAG GDLLFIEATK MAGKGGMTLT GQLGDVMKES
ATAALSYLRS KAEQLGISPN FLEKTDLHLH FPAGSIPKDG PSAGVTILTA LTSLLTGIRV
RHDTAMTGEA TLRGLVLPVG GIKEKVLAAH RAGIKRVILP ERCRKDLIDV PDQARNELEF
IFVTHMDDVL KAALETPPVG VAGTPGGEPG KEAPLPKPAE SAPEVRA
