ID A0A0A8JJ15_BACSX Unreviewed; 348 AA.
AC A0A0A8JJ15;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=OXB_1940 {ECO:0000313|EMBL:BAQ10411.1};
OS Bacillus sp. (strain OxB-1).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=98228 {ECO:0000313|EMBL:BAQ10411.1, ECO:0000313|Proteomes:UP000031651};
RN [1] {ECO:0000313|Proteomes:UP000031651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OxB-1 {ECO:0000313|Proteomes:UP000031651};
RA Yamaguchi T., Asano Y.;
RT "Complete genome of an aldoxime degrader Bacillus sp. OxB-1.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAQ10411.1, ECO:0000313|Proteomes:UP000031651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OxB-1 {ECO:0000313|EMBL:BAQ10411.1,
RC ECO:0000313|Proteomes:UP000031651};
RA Yamaguchi T., Asano Y.;
RT "Complete Genome Sequence of an Aldoxime Degrader, Bacillus sp. OxB-1.";
RL Genome Announc. 3:e00025-15(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 -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01122}.
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DR EMBL; AP013294; BAQ10411.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A8JJ15; -.
DR STRING; 98228.OXB_1940; -.
DR KEGG; baco:OXB_1940; -.
DR HOGENOM; CLU_042037_2_0_9; -.
DR OrthoDB; 2356897at2; -.
DR Proteomes; UP000031651; Chromosome.
DR GO; GO:0005524; F:ATP binding; 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 Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; NF041438; SepM_fam_S16; 1.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF48; ENDOPEPTIDASE LA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Reference proteome {ECO:0000313|Proteomes:UP000031651};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 120..186
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 229..345
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 234
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 279
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 348 AA; 38117 MW; D46C8C23758307A0 CRC64;
MRMKRLGLLL AILAILAAVL FYPMDTYISK PGGAYELSPF VKVQGGDEDD IGTFSLMTIS
VSKATPATYL YAKFSDYQKL LPSYKVRRHG ENDKEYTTRQ KKLMSDSQFN AIHVAYQKTG
FPLKVDFDGV FVIMVLPGGA ADGKLEVGDK IHAVDGVPLK ETGQFASLIA GKGEGDDVHL
TIEREKEEKL IVLSMKEIPG NDGRIGLGIQ FQEDRTLTTD PKVDFHTADI GGPSAGLMFT
LEIMNQLLDE DLTKGYNIAG TGEMLEDGTV GRIGGADFKV VAADRKGVEI FFAPDDDLPD
EVRESNPGVM TNYEEAVKMA EKIGTKMKIV PVKTVDDALA YLQTLEEK
//
