ID D4FW99_BACNB Unreviewed; 332 AA.
AC D4FW99;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 2.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN Name=ylbL {ECO:0000313|EMBL:BAI85130.2};
GN ORFNames=BSNT_08013 {ECO:0000313|EMBL:BAI85130.2};
OS Bacillus subtilis subsp. natto (strain BEST195).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=645657 {ECO:0000313|EMBL:BAI85130.2, ECO:0000313|Proteomes:UP000006805};
RN [1] {ECO:0000313|EMBL:BAI85130.2, ECO:0000313|Proteomes:UP000006805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BEST195 {ECO:0000313|EMBL:BAI85130.2,
RC ECO:0000313|Proteomes:UP000006805};
RX PubMed=20398357; DOI=10.1186/1471-2164-11-243;
RA Nishito Y., Osana Y., Hachiya T., Popendorf K., Toyoda A., Fujiyama A.,
RA Itaya M., Sakakibara Y.;
RT "Whole genome assembly of a natto production strain Bacillus subtilis natto
RT from very short read data.";
RL BMC Genomics 11:243-243(2010).
RN [2] {ECO:0000313|EMBL:BAI85130.2, ECO:0000313|Proteomes:UP000006805}
RP GENOME REANNOTATION.
RC STRAIN=BEST195 {ECO:0000313|EMBL:BAI85130.2,
RC ECO:0000313|Proteomes:UP000006805};
RX PubMed=25329997; DOI=10.1371/journal.pone.0109999;
RA Kamada M., Hase S., Sato K., Toyoda A., Fujiyama A., Sakakibara Y.;
RT "Whole genome complete resequencing of Bacillus subtilis natto by combining
RT long reads with high-quality short reads.";
RL PLoS ONE 9:E109999-E109999(2014).
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; AP011541; BAI85130.2; -; Genomic_DNA.
DR AlphaFoldDB; D4FW99; -.
DR STRING; 86029.AWV81_08390; -.
DR KEGG; bso:BSNT_08013; -.
DR HOGENOM; CLU_042037_2_0_9; -.
DR Proteomes; UP000006805; 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 CDD; cd00986; PDZ_LON_protease; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR039381; La_PDZ.
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 Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 91..177
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 178..327
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 225
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 270
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 332 AA; 36437 MW; 393F74F41FAEEA66 CRC64;
MLVILILIAV LSFIKLPYYI TKPGEATELA SLIKVEGGYP EKGSLSLMTV KVGPANPFTY
VWAKMHPYYE IVPDESIKEE GESDKEYMKR QLQMMKSSQE NAVIAAYQKA GKKVSYSFNG
IYASSVVENM PAKGKIEVGD KIISADGKNY QSAEKLIDYI SSKKAGDKVT LKIEREEKEK
RVTLTLKQFP DEPDRAGIGV SLYTDRNVKV EPDIDFEIEN IGGPSAGLMM SLEIYNQLTK
PDETKGYDIA GTGTIDVDGK VGPIGGIDQK VVAADKAGKD IFFAPNQNGA SNSDYKNAVK
TAKDIDSNMK IVPVDTMQDA IDYLNKLKAK ST
//
