ID A0A1C4VA58_MICVI Unreviewed; 332 AA.
AC A0A1C4VA58;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=GA0074695_1269 {ECO:0000313|EMBL:SCE80681.1};
OS Micromonospora viridifaciens.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1881 {ECO:0000313|EMBL:SCE80681.1, ECO:0000313|Proteomes:UP000198242};
RN [1] {ECO:0000313|EMBL:SCE80681.1, ECO:0000313|Proteomes:UP000198242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43909 {ECO:0000313|EMBL:SCE80681.1,
RC ECO:0000313|Proteomes:UP000198242};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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; LT607411; SCE80681.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4VA58; -.
DR OrthoDB; 2356897at2; -.
DR Proteomes; UP000198242; Chromosome i.
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 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 125..187
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; 34320 MW; AB22DDCE8B7EFD39 CRC64;
MTVLLGALLT ALLSIGALTV PIPYVVLGPG PTVNTLGSSD GKEIIQVTGR PTSTSAGQLR
LTTVGVQPTV RLRSALAGWF SKDEAVVPRE LVYPPGESQQ EVEKRNAEDF QNSQTSAETA
ALRKLGYPVQ VLVKAVTAGG PSVGVLKPGD VLTSVDGQAV TSAARLTELI RARPAGSALK
IGYTRDGQPG TATVTSREQD GRPRIGVEID QQQPHPFTLK IDLADIGGPS AGLMFALGVI
DKLEPADLTG GKIIAGTGTI DDEGRVGPIG GIAQKLVGAK QAGAKVFLVP ADNCAEAVRN
PQPDLPLLKV ATLDDALKAL ETLRAGGQPP RC
//
