ID A0A0X3VBJ6_9ACTN Unreviewed; 364 AA.
AC A0A0X3VBJ6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=ADL22_14515 {ECO:0000313|EMBL:KUL41787.1};
OS Streptomyces sp. NRRL F-4489.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609095 {ECO:0000313|EMBL:KUL41787.1, ECO:0000313|Proteomes:UP000053256};
RN [1] {ECO:0000313|EMBL:KUL41787.1, ECO:0000313|Proteomes:UP000053256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-4489 {ECO:0000313|EMBL:KUL41787.1,
RC ECO:0000313|Proteomes:UP000053256};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUL41787.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LLZI01000169; KUL41787.1; -; Genomic_DNA.
DR RefSeq; WP_066978314.1; NZ_LLZI01000169.1.
DR AlphaFoldDB; A0A0X3VBJ6; -.
DR STRING; 1609095.ADL22_14515; -.
DR OrthoDB; 2356897at2; -.
DR Proteomes; UP000053256; 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 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.
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:UP000053256};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 249..348
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 254
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 300
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 364 AA; 37860 MW; 78FA7E4E71E03F63 CRC64;
MPRRTATLLA SILMLIALLC AGVLIPVPYA EMSPGPTVNT LGEHNGEPVL QISGRKTYPT
SGHLNMTTVR VTGPDYRMNL LEAVYGWLDP DSAVVPHKTL YPEGQTAEQA DQQNAEEFSQ
SQESAKAAAL KQLHIPVATQ TVVGTVVKGK PADGLLHAGD VIKAVDGQEV RQTGDVAKLV
TRHKPGEKVV FTVIPAKEAA AAEKQGKRPE GPGKQVAITT AADGGRAIVG IQAQLDHIFP
FPIDVKLADV GGPSAGLMFA LGIVDKLTPG GDLTGGTFVA GTGTIDDQGK VGPIGGISMK
TIGARDKGAQ FFLTPKENCA AAAKDTPSGL RLVKVGSIED AVQALAKIRK KDLADLPSCT
PAGH
//
