ID W0EFV0_9FIRM Unreviewed; 576 AA.
AC W0EFV0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=DESME_13620 {ECO:0000313|EMBL:AHF07951.1};
OS Desulfitobacterium metallireducens DSM 15288.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=871968 {ECO:0000313|EMBL:AHF07951.1, ECO:0000313|Proteomes:UP000010847};
RN [1] {ECO:0000313|EMBL:AHF07951.1, ECO:0000313|Proteomes:UP000010847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15288 {ECO:0000313|Proteomes:UP000010847};
RG DOE Joint Genome Institute;
RA Smidt H., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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; CP007032; AHF07951.1; -; Genomic_DNA.
DR RefSeq; WP_006715796.1; NZ_CP007032.1.
DR AlphaFoldDB; W0EFV0; -.
DR STRING; 871968.DESME_13620; -.
DR MEROPS; S16.005; -.
DR KEGG; dmt:DESME_13620; -.
DR eggNOG; COG1067; Bacteria.
DR eggNOG; COG1474; Bacteria.
DR HOGENOM; CLU_020014_0_0_9; -.
DR OrthoDB; 2318150at2; -.
DR Proteomes; UP000010847; 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 GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; IPR002078; Sigma_54_int.
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.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000010847};
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..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 94..267
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT DOMAIN 350..539
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 448
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 491
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 576 AA; 62272 MW; DEA5729C06BA61C0 CRC64;
MSGLSGVVMI VQLIFAVVIG MYFWGMLKAQ QGNKVSVEKE SRKELEKLEK MRKIQLSTPL
AEKTRPQHFI DIVGQKEGIK ALQAALCGPN PQHVLIYGPP GIGKTAAARL VLEEAKKNPL
SPFKEFSKFI EIDGATARFD ERGIADPLIG SVHDPIYQGA GAMGMAGIPQ PKAGAVTKAH
GGVLFIDEIG ELHPIQINKL LKVLEDRKVI LESAYYSSED TNIPAHIHDI FQNGLPADFR
LVGATTRSPE EIPPAIRSRC MEIYFRVLLP DEIGAIARGA AAKMEIPMTE GAVEVAKHYA
TNGREAVNIV QLAAGVAQAD KLFEITAATI EWVVNSGQYA PRPERKVPTE AEIGVVNGLA
VYGPNMGMLL ELEVTAQPVS AGTGALLVTG IVEEEEQGSS TKKIRRKSMA RSSVENVLTV
LRRQLSIDFR NYDIHVNFPG GVPLDGPSAG VAIATAVVSA VRKQRVDNYL AMTGELSIRG
AVKPVGGIVA KLEAAHQAGC RRAFIPKENW QERFRALADG FQVIPVESLA EVLKAAFLSE
PGKSNLEIQP PLEEVLARLE INPIPPVNLP ERGQSC
//
