ID A0A2U3P3A9_9MYCO Unreviewed; 332 AA.
AC A0A2U3P3A9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=MNAB215_430 {ECO:0000313|EMBL:SPM38253.1};
OS Mycobacterium numidiamassiliense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1841861 {ECO:0000313|EMBL:SPM38253.1, ECO:0000313|Proteomes:UP000240424};
RN [1] {ECO:0000313|EMBL:SPM38253.1, ECO:0000313|Proteomes:UP000240424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB215 {ECO:0000313|EMBL:SPM38253.1,
RC ECO:0000313|Proteomes:UP000240424};
RG Urmite Genomes;
RL Submitted (JAN-2017) 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; FUEZ01000003; SPM38253.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U3P3A9; -.
DR STRING; 1841861.GCA_900157365_04633; -.
DR Proteomes; UP000240424; Unassembled WGS sequence.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000240424};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 104..182
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 225..323
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 230
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 275
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 332 AA; 34216 MW; 17B781F38A6F7EB1 CRC64;
MVALVPILVF GVLLAVVTVP FVSLGPGPTF DTLGEVDGKE VVAIAGTQTH PTTGHLNMTT
VSQRDDLTLG EALTLWLSGQ EQLVPRDLIY PPGKSRDDVD KSNNADFKQS EDSAAYAALG
YLNYAPAVTV ATVTDPGPSA GQLKPGDAID AVNGTPTSNV EQFTGLLKNT KPGQVVTIDF
RRKNEPAGVA QITLGTNKDR DYGFMGVAVL DAPWAPFVVD FNLANVGGPS AGLMFSLAVV
DKLTTGGLAG SMFIAGTGTI SSDGKVGQIG GITHKMVAAH AAGATVFLVP AKNCYEANSD
NPSGLRLVKV ETLSQAVDAL HAVTAGGQPP SC
//
