ID A0A0F2PXC8_9FIRM Unreviewed; 570 AA.
AC A0A0F2PXC8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=VR69_02075 {ECO:0000313|EMBL:KJS18120.1};
OS Peptococcaceae bacterium BRH_c4b.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=1629717 {ECO:0000313|EMBL:KJS18120.1, ECO:0000313|Proteomes:UP000033446};
RN [1] {ECO:0000313|EMBL:KJS18120.1, ECO:0000313|Proteomes:UP000033446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c4b {ECO:0000313|EMBL:KJS18120.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJS18120.1}.
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DR EMBL; LADO01000007; KJS18120.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2PXC8; -.
DR STRING; 1629717.VR69_02075; -.
DR PATRIC; fig|1629717.3.peg.139; -.
DR Proteomes; UP000033446; 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 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; 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; PS01046; LON_SER; 1.
DR PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122};
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..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 354..542
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 452
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 495
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 570 AA; 60902 MW; 37779E1575B9679A CRC64;
MGEAGIGIGS FLTFIQVFFA VIIGMYFWNM LKAQQGNKSA VERESRKELE KLQRLRAISL
TEPLAEKTRP TSFKEIIGQS EGLKSLRAAL CGPNPQHVII YGPPGVGKTA AARVVLEEAK
KNTSSPFKVD AKFIEMDATT ARFDERGIAD PLIGSVHDPI YQGAGPLGMA GVPQPKAGAV
TKAHGGMLFL DEIGELHHIQ MNKLLKVMED RKVLLESAYY SSEDNNIPGH IHDIFQNGLP
ADFRLVGATT RTPEDIAPAI RSRCLEVFFK PLQPEEIELI AANASEKVGF PMAGGCLEVI
KKYATSGREA VNIIQIAAGI AMTEGRKTIS TCDVEWVVNS GQYSPRPEKK VASQPQIGLV
NGLAVYGPNT GTLLEIEAGA VPVARGQGKV IVTGVVEEEE IGGRGRTIRR KSMAKGSIEN
VLTVLRRVSD VNPPDYDIHV NFPGGVPIDG PSAGVAVAAA VYSAIKGIPV DNRLAMTGEI
SIRGLVLPVG GVVSKVEAAR RAGASRVLIP AENYQETFRD LEGVKVLPVT RLEQVLKDAL
VEDPGLTNPA PVVVKADVLV AAGVQGVNCH
//
