ID A0A2G5J096_9ACTN Unreviewed; 364 AA.
AC A0A2G5J096;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=B1C81_07585 {ECO:0000313|EMBL:PIB10349.1};
OS Streptomyces sp. HG99.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1958787 {ECO:0000313|EMBL:PIB10349.1, ECO:0000313|Proteomes:UP000231274};
RN [1] {ECO:0000313|EMBL:PIB10349.1, ECO:0000313|Proteomes:UP000231274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HG99 {ECO:0000313|EMBL:PIB10349.1,
RC ECO:0000313|Proteomes:UP000231274};
RA Li Y.;
RT "Diversity and bioprospecting of biosynthetic gene clusters of culturable
RT actinobacteria from Tibetan Plateau, China.";
RL Submitted (FEB-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}.
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:PIB10349.1}.
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DR EMBL; MVDM01000003; PIB10349.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5J096; -.
DR Proteomes; UP000231274; 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:UP000231274};
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 REGION 102..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 257
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 302
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 364 AA; 38236 MW; ED3366FEE39DC324 CRC64;
MPRRTATMLA STLILIALLC AGVFIKVPYS EMSPGPTVNT LGEHDGEPVL QISGRKTYPT
TGHLNMTTVR VTSADYNMNL VEAVYGWLAH DNRVVPHDTL YPDGKTEEQS TQENAEEFSQ
SQESAKVAAL KELDIPVKSW VIVSTVLKGS PAEGRLHAGD VIKAVDGTTV KAPDDVAKLV
TEHKPGDKVV FTIVPAKEQA AAEKENKTAT VTKDVTITTA KSDDGGTDRA IVGISAGTDH
TFPFTIDIKL ADVGGPSAGL MFALGIVDKL TPGNLTGGTF VAGTGTIDDN GKVGPIGGIA
MKTVGAREKG AQYFLTPKDN CAAAAMDTPE GLTLVKVDTI DDAMSALKDI NSGRTADLPE
CTTK
//
