ID A0QTT6_MYCS2 Unreviewed; 345 AA.
AC A0QTT6;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 93.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN OrderedLocusNames=MSMEG_1958 {ECO:0000313|EMBL:ABK74188.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196 {ECO:0000313|EMBL:ABK74188.1, ECO:0000313|Proteomes:UP000000757};
RN [1] {ECO:0000313|EMBL:ABK74188.1, ECO:0000313|Proteomes:UP000000757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000000757};
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) 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; CP000480; ABK74188.1; -; Genomic_DNA.
DR RefSeq; YP_886324.1; NC_008596.1.
DR AlphaFoldDB; A0QTT6; -.
DR STRING; 246196.MSMEG_1958; -.
DR MEROPS; S16.012; -.
DR PaxDb; 246196-MSMEI_1914; -.
DR KEGG; msm:MSMEG_1958; -.
DR PATRIC; fig|246196.19.peg.1936; -.
DR eggNOG; COG3480; Bacteria.
DR OMA; TDHTFPF; -.
DR OrthoDB; 2356897at2; -.
DR Proteomes; UP000000757; 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; 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.
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:UP000000757};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 141..195
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 238..336
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 243
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 288
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 345 AA; 36183 MW; 89D446B97606DCF3 CRC64;
MNGVNRRILT LLVALVPVVA FGVLLSVVQV PFVSLGPGPT FNTLGEIDGK QVVDIEGPDA
TVHPTSGHLN MTTVSQRDGL TLGQAITLWM SGREQLVPRD LVYPPDKSKD EIDEANTADF
KNSEDSAEYA ALSFLKYPMA VTVQNVTDPG PSAGKLQDGD AIDGVNGKPV ANLDEFQALL
KETKPGDKLV IDYRRKNAPP GEATITLGDN PDRDYGYLGI AVLDAPWAPF DIEFNLANIG
GPSAGLMFSL AVVDKLTTGD LNDGKFIAGT GTISGDGKVG SIGGITHKML AASEAGAEVF
LVPADNCTEA RSAPRDGLEL VKVETLEGAV DALKTISAGG EPPRC
//