ID A0A1W1XL74_9CLOT Unreviewed; 564 AA.
AC A0A1W1XL74;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=SAMN02745134_02286 {ECO:0000313|EMBL:SMC24733.1};
OS Clostridium acidisoli DSM 12555.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121291 {ECO:0000313|EMBL:SMC24733.1, ECO:0000313|Proteomes:UP000192468};
RN [1] {ECO:0000313|EMBL:SMC24733.1, ECO:0000313|Proteomes:UP000192468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12555 {ECO:0000313|EMBL:SMC24733.1,
RC ECO:0000313|Proteomes:UP000192468};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FWXH01000007; SMC24733.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1XL74; -.
DR STRING; 1121291.SAMN02745134_02286; -.
DR Proteomes; UP000192468; Unassembled WGS sequence.
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 CDD; cd18139; HLD_clamp_RarA; 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; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
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; PS00676; SIGMA54_INTERACT_2; 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:UP000192468};
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 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 94..260
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT DOMAIN 351..539
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 449
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 492
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 564 AA; 62414 MW; F083F260A9FDFEBD CRC64;
MPKNMTMLLL VVELFFTVII GIYFFTLLKG QQSSKIVIDK ENKKEMDNLN KLRSISLTMP
LTEKSRPKTF DEIIGQEKGI KALKAAICGP NPQNVIIYGP PGVGKTAAAR LVLEYAKKIN
YSPFKSEAKF IEIDATTVRF DDRGIADPLI GSVHDPIYQG AGSLGIAGIP QPKSGAVTKA
HGGILFIDEI GELHPTEMNK LLKVLEDRKV FLDSAYYNSS DNKMPVYIKE IFENGLPADF
RLVGATTRSP EEICPALRSR CVEIFFKPLL PDELKRIALN AVEKVEMKIE KKALEMVSEY
SNNGRDAVNL IQLAYGIVLN EKRDKVRLGD VEWVIENGQY SPKIEKKINE KPQIGYVNGL
AIYGANIGTI MEIEASAIKI KNNDGKLKVT GIVEEEEIKN GNNKIIRKSN ARCSVENVIT
MLERKFNINC NEYNIHVNFP GGAPVDGPSA GISMATAIYS AIKGVYVDNR IAMTGEISLY
GKVKPVGGVD AKIAAAIKAG AKIIIIPREN WQDKFNRING VKIKPVDSIN EVFDLSITDK
IEDNNITFET KGEILLAKLN EYKC
//
