ID I3E542_BACMT Unreviewed; 340 AA.
AC I3E542;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=PB1_01690 {ECO:0000313|EMBL:EIJ81613.1};
OS Bacillus methanolicus PB1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=997296 {ECO:0000313|EMBL:EIJ81613.1, ECO:0000313|Proteomes:UP000010523};
RN [1] {ECO:0000313|EMBL:EIJ81613.1, ECO:0000313|Proteomes:UP000010523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB1 {ECO:0000313|EMBL:EIJ81613.1,
RC ECO:0000313|Proteomes:UP000010523};
RX PubMed=22610424; DOI=10.1128/AEM.00703-12;
RA Heggeset T.M., Krog A., Balzer S., Wentzel A., Ellingsen T.E.,
RA Brautaset T.;
RT "Genome Sequence of Thermotolerant Bacillus methanolicus: Features and
RT Regulation Related to Methylotrophy and Production of L-Lysine and L-
RT Glutamate from Methanol.";
RL Appl. Environ. Microbiol. 78:5170-5181(2012).
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}.
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:EIJ81613.1}.
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DR EMBL; AFEU01000001; EIJ81613.1; -; Genomic_DNA.
DR RefSeq; WP_003350332.1; NZ_AFEU01000001.1.
DR AlphaFoldDB; I3E542; -.
DR STRING; 997296.PB1_01690; -.
DR PATRIC; fig|997296.3.peg.387; -.
DR eggNOG; COG3480; Bacteria.
DR OrthoDB; 2356897at2; -.
DR Proteomes; UP000010523; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 120..186
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 229..336
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 340 AA; 37996 MW; AF69451D99BC7FCD CRC64;
MSRKIYIRNF LIAAIILLAS SFYYLPYYVS KPGMAKELEP IIEVDGGYDE EGSLMLTTVR
MGRANIYSYI LAKLSKYQEI FPAEMIKYEH ETDEEYALRQ LRAMDTSKLS AIEVAYKKAG
IPVEYRYKGV YVMSVLPDMP AEGKLKPGDR IFKINDVMFK SSDEFKQYVS KKKKGDMIQI
SYVRNGKANR TMLQVMPFPD NRDQLGIGIV LEDDKEIIVE PDVKVNTDEI GGPSAGLMFA
LEIYNQLTED DLTQGFDIAG TGTISPDGTV GRIGGIEQKI VAADKAGADI FLAPNEKGAH
GSNYEIAVKT ATDIGTDMKI VPVDTFDDAV FYLENLKEKK
//
