ID I3ECS2_BACMM Unreviewed; 555 AA.
AC I3ECS2;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN Name=lon2 {ECO:0000313|EMBL:AIE60936.1};
GN ORFNames=BMMGA3_12715 {ECO:0000313|EMBL:AIE60936.1};
OS Bacillus methanolicus (strain MGA3 / ATCC 53907).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=796606 {ECO:0000313|EMBL:AIE60936.1, ECO:0000313|Proteomes:UP000027602};
RN [1] {ECO:0000313|EMBL:AIE60936.1, ECO:0000313|Proteomes:UP000027602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGA3 / ATCC 53907 {ECO:0000313|Proteomes:UP000027602};
RX PubMed=25758049;
RA Irla M., Neshat A., Brautaset T., Ruckert C., Kalinowski J., Wendisch V.F.;
RT "Transcriptome analysis of thermophilic methylotrophic Bacillus
RT methanolicus MGA3 using RNA-sequencing provides detailed insights into its
RT previously uncharted transcriptional landscape.";
RL BMC Genomics 16:73-73(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01122};
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC {ECO:0000256|ARBA:ARBA00026070}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01122}.
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DR EMBL; CP007739; AIE60936.1; -; Genomic_DNA.
DR RefSeq; WP_003347586.1; NZ_CP007739.1.
DR AlphaFoldDB; I3ECS2; -.
DR STRING; 796606.BMMGA3_12715; -.
DR MEROPS; S16.005; -.
DR KEGG; bmet:BMMGA3_12715; -.
DR eggNOG; COG0470; Bacteria.
DR eggNOG; COG1067; Bacteria.
DR HOGENOM; CLU_020014_0_0_9; -.
DR OrthoDB; 2318150at2; -.
DR Proteomes; UP000027602; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008268; Peptidase_S16_AS.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR014251; Spore_LonB.
DR NCBIfam; TIGR02902; spore_lonB; 1.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF64; LON PROTEASE; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF01078; Mg_chelatase; 1.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122,
KW ECO:0000313|EMBL:AIE60936.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000027602};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 349..535
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 445
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 488
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 555 AA; 60909 MW; A40627CE0DE39DCA CRC64;
MSWTGIALFI QLFFGIIIGL YFWNLLRSQR TQKVSIDRES KKEMEQLKKM RSISLTEPLS
EKVRPSRFED IVGQEDGIKS LKAALCGPNP QHVIIYGPPG VGKTAAARLV LEEAKKNQKS
PFQRSSVFIE LDATTARFDE RGIADPLIGS VHDPIYQGAG AMGQAGIPQP KQGAVTNAHG
GVLFIDEIGE LHPIQMNKLL KVLEDRKVFL ESAYYNEENT QIPTHIHDIF KNGLPADFRL
VGATTRTPNE IPPAIRSRCI EVFFRDLNQE EIAVVAKKAA EKVRLSITEQ GLNILSTYAR
NGREAVNMVQ TAAGLAINED RNYIKDEDIE WVINSSQLSP RIEKKIHPKS NIGLVNGLAV
YGPNIGALLE IEVTVIPAKE KGSINITGIV EEESIGDRGK SIRRKSMARG SIENVITVLR
SMKVPADEFD IHVNFPGGIP IDGPSAGIAM ATAIYSAIYK IPVNNTIAMT GEISIHGKVK
PIGGVYPKVV AAKKAGAKTV IIPEENMQSI LNEIKDIKIV PVTHLNEVFD LAFVKGKPRD
QAIQASIELA KKESI
//
