ID S3ZY98_9ACTN Unreviewed; 356 AA.
AC S3ZY98;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=STRAU_3532 {ECO:0000313|EMBL:EPH43410.1};
OS Streptomyces aurantiacus JA 4570.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=1286094 {ECO:0000313|EMBL:EPH43410.1, ECO:0000313|Proteomes:UP000014629};
RN [1] {ECO:0000313|EMBL:EPH43410.1, ECO:0000313|Proteomes:UP000014629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA 4570 {ECO:0000313|EMBL:EPH43410.1,
RC ECO:0000313|Proteomes:UP000014629};
RA Gruening B.A., Praeg A., Erxleben A., Guenther S., Mueller M.;
RT "Draft Genome Sequence of Streptomyces aurantiacus, Which Produces
RT Setomimycin.";
RL Submitted (FEB-2013) 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:EPH43410.1}.
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DR EMBL; AOPZ01000163; EPH43410.1; -; Genomic_DNA.
DR AlphaFoldDB; S3ZY98; -.
DR PATRIC; fig|1286094.4.peg.3494; -.
DR Proteomes; UP000014629; 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.
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:UP000014629};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 134..167
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 243..341
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 248
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 293
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 356 AA; 37142 MW; C7B0139DFE608258 CRC64;
MLASTLMLIA LLCAGVLIKV PYSEMSPGPT VNTLGDHDGE PVLQISGRKT YATSGHLNMT
TVRVTSADYK MNLAEAVYGW MAHDNIVVPH DTLYPDGKTE QQSTQENAEE FSQSQESAKV
AALKELKIPV KSQVVVATVF KDSPAEGKLH AGDVIKSVDG TAVKEFTDVA KLVTKHKPGE
PVVFGVVPVK EAAAAEKAGK EPAASETVKM TTEKAEDDGR AVVGIKAGTD HTYPFTIDIK
LADVGGPSAG LMFALGIVDK LTPGDLTGGK FVAGTGTIDD TGKVGPIGGI EMKTVGARDK
GAEYFLTPKD NCASAASDVP DGLTLVKVDT IDDAVKSLKA ISKGDTADLP KCTTKG
//
