ID L1KPN9_9ACTN Unreviewed; 365 AA.
AC L1KPN9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=STRIP9103_06589 {ECO:0000313|EMBL:EKX62529.1};
OS Streptomyces ipomoeae 91-03.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=698759 {ECO:0000313|EMBL:EKX62529.1, ECO:0000313|Proteomes:UP000010411};
RN [1] {ECO:0000313|EMBL:EKX62529.1, ECO:0000313|Proteomes:UP000010411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91-03 {ECO:0000313|EMBL:EKX62529.1,
RC ECO:0000313|Proteomes:UP000010411};
RA Huguet-Tapia J.C., Durkin A.S., Pettis G.S., Badger J.H.;
RL Submitted (NOV-2012) 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:EKX62529.1}.
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DR EMBL; AEJC01000511; EKX62529.1; -; Genomic_DNA.
DR RefSeq; WP_009327785.1; NZ_AEJC01000511.1.
DR AlphaFoldDB; L1KPN9; -.
DR PATRIC; fig|698759.3.peg.6775; -.
DR OrthoDB; 2356897at2; -.
DR Proteomes; UP000010411; 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:UP000010411};
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; 38286 MW; D8C9E43DB280FEE7 CRC64;
MPRRTATMLA STLMLIALLC AGVLIPVPYS EMSPGPTVNT LGEHDGEPVL QISGHKTYPA
TGHLNMTTVR VTSADYKMNL VEAVYGWLAH DNKVVPHDTL YPNGKTEEES TQENAEEFSQ
SQESAKVAAL KELDIPVKSW VIVSTVLKGS PAEGKLHAGD VIKSVDGTAV KAPEDVATLV
TKHKPGEDVD FVIVPAKAQA AAEKQNKTAT ETEKVTITTA KSDDSGEDRA IVGISAGTDH
TFPFTVDIKL ADVGGPSAGL MFALGIYDKL TPGNLTGGKF VAGTGTIDDE GKVGPIGGIE
MKTVGARSKG AQYFLTPKDN CAAAAKDTPD GLTLVKVDTI DDALNALEDI RSGDTADLPK
CTTKG
//
