ID A0A0P6W8B3_9BACI Unreviewed; 347 AA.
AC A0A0P6W8B3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=AM506_00965 {ECO:0000313|EMBL:KPL61237.1};
OS Rossellomorea vietnamensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX NCBI_TaxID=218284 {ECO:0000313|EMBL:KPL61237.1, ECO:0000313|Proteomes:UP000050398};
RN [1] {ECO:0000313|EMBL:KPL61237.1, ECO:0000313|Proteomes:UP000050398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-SED5 {ECO:0000313|EMBL:KPL61237.1,
RC ECO:0000313|Proteomes:UP000050398};
RA Lee R.D., Jospin G., Lang J.M., Coil D.A., Eisen J.A.;
RT "Draft Genome Sequence of Bacillus vietnamensis UCD-SED5.";
RL Submitted (AUG-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 -!- 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:KPL61237.1}.
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DR EMBL; LIXZ01000001; KPL61237.1; -; Genomic_DNA.
DR RefSeq; WP_060669920.1; NZ_LIXZ01000001.1.
DR AlphaFoldDB; A0A0P6W8B3; -.
DR PATRIC; fig|218284.4.peg.200; -.
DR eggNOG; COG3480; Bacteria.
DR OrthoDB; 2356897at2; -.
DR Proteomes; UP000050398; 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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Reference proteome {ECO:0000313|Proteomes:UP000050398};
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 100..161
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 228..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 347 AA; 38946 MW; 753EC4308DC7B5FB CRC64;
MKTKTLIRIL LIMTIVMVAT SFYYLPFYVT KPGSAHELDP IVHVENGYED DGELMLTTVR
MGRANIYAYL MASIRKYEYI FPVEEIRSPH ESDEEYNLRQ LQLMNNSQSH AIEVAYSKAG
KPYEYKYKGI YVLNIYPDMP AEKVLKPGDR ITAIDGQTFQ SSQEFIDYVS GKTKGDKVDI
TFVRDKEERV EAIPLEAFPD VPDKIGLGIT LSDDKEIITD PPVKLETEEI GGPSAGLMFS
LEIYDQLTEG DLAKGHRIAG TGTISEDGTV GRIGGIEQKI IAADKADAEY FLAPDETITK
EMKKKYPDLE SNYTAAKRTA EDIGTDMKVI PVKTFDEALS FLKSIKN
//
