ID A0A0X3XJ16_9ACTN Unreviewed; 365 AA.
AC A0A0X3XJ16;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=ADL34_29825 {ECO:0000313|EMBL:KUL69867.1};
OS Streptomyces sp. NRRL WC-3605.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609103 {ECO:0000313|EMBL:KUL69867.1, ECO:0000313|Proteomes:UP000052945};
RN [1] {ECO:0000313|EMBL:KUL69867.1, ECO:0000313|Proteomes:UP000052945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3605 {ECO:0000313|EMBL:KUL69867.1,
RC ECO:0000313|Proteomes:UP000052945};
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:KUL69867.1}.
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DR EMBL; LLZN01000091; KUL69867.1; -; Genomic_DNA.
DR RefSeq; WP_062673982.1; NZ_LLZN01000091.1.
DR AlphaFoldDB; A0A0X3XJ16; -.
DR OrthoDB; 2356897at2; -.
DR Proteomes; UP000052945; 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; 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:UP000052945};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 141..171
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 252..350
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 257
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 302
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 365 AA; 38309 MW; 10E05B982E546A81 CRC64;
MPRRTATMLA STLMLIALLC AGVFIRVPYA EMSPGPTVNT LGEHDGEPVL QITGRKTYPT
TGHLNMTTVR VTSADYRMNL VEAVYGWLAH DNKVVPHDTL YPDGKTEEES TQENAEEFSQ
SQESAKVAAL EALDIPVRSW VIVSTVVKGS PAEGELHAGD VIKAVDGTAV KKPGDVAELV
TKHKPGQKVV FTIVPAKEQA AAEKERRSPQ GTEKVTITTA ESHDSGAKRA IVGISAGTDH
TFPFDIDIKL ADVGGPSAGL MFALGLYDKL TPGSLTGGKF VAGTGTIDDA GKVGPIGGIE
MKTVGARDKG AQYFLTPADN CATAARDVPD GLTLVKVDTI DDALGALKDI RSGDTAALPK
CTTGS
//
