ID A0A448I9L2_MYCCI Unreviewed; 333 AA.
AC A0A448I9L2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
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:VEG49108.1};
GN ORFNames=NCTC10485_03414 {ECO:0000313|EMBL:VEG49108.1};
OS Mycolicibacterium chitae (Mycobacterium chitae).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1792 {ECO:0000313|EMBL:VEG49108.1, ECO:0000313|Proteomes:UP000282551};
RN [1] {ECO:0000313|EMBL:VEG49108.1, ECO:0000313|Proteomes:UP000282551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10485 {ECO:0000313|EMBL:VEG49108.1,
RC ECO:0000313|Proteomes:UP000282551};
RG Pathogen Informatics;
RL Submitted (DEC-2018) 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}.
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DR EMBL; LR134355; VEG49108.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A448I9L2; -.
DR Proteomes; UP000282551; Chromosome 1.
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; cd00987; PDZ_serine_protease; 1.
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 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 SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 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:UP000282551};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 226..324
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 231
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 276
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 333 AA; 34688 MW; 2008AB7DD22F4CA1 CRC64;
MLVALVPILA FGVLLAAVTV PFVSLGPGPI FNTLGDFDGK PVIEIEGTDV EPTAGELNMT
TVSQRDGLTL GQAMTLWLSG REQLLPRDLV YPPDKTRDDI DKANQAEFKS SEDSAEYAAL
SFLDYPRAVT VETVSDDGPA KDKLRDGDAI DAVNGTPVAD VAAFTGLLEH TKPGDDIVVD
FRRKNEAPGT VTITLGSNDD RDYGYVGVGV RDAPWAPFTI DFNLANIGGP SAGLMFSLAV
VDKLTPGELN DGRNVAGSGT IDGDGKVGSI GGITHKLAAA REAGATVFLV PADNCAEAVS
AKQDGMELVK VETLDSAVAA LETVSAGGEP PRC
//
