ID A4F8Q7_SACEN Unreviewed; 333 AA.
AC A4F8Q7;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN OrderedLocusNames=SACE_1100 {ECO:0000313|EMBL:CAM00432.1};
GN ORFNames=A8924_1494 {ECO:0000313|EMBL:PFG94227.1};
OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=405948 {ECO:0000313|EMBL:CAM00432.1, ECO:0000313|Proteomes:UP000006728};
RN [1] {ECO:0000313|EMBL:CAM00432.1, ECO:0000313|Proteomes:UP000006728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC {ECO:0000313|EMBL:CAM00432.1};
RX PubMed=17369815; DOI=10.1038/nbt1297;
RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA Haydock S.F., Leadlay P.F.;
RT "Complete genome sequence of the erythromycin-producing bacterium
RT Saccharopolyspora erythraea NRRL23338.";
RL Nat. Biotechnol. 25:447-453(2007).
RN [2] {ECO:0000313|EMBL:PFG94227.1, ECO:0000313|Proteomes:UP000225825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG94227.1,
RC ECO:0000313|Proteomes:UP000225825};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (SEP-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}.
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DR EMBL; AM420293; CAM00432.1; -; Genomic_DNA.
DR EMBL; PDBV01000001; PFG94227.1; -; Genomic_DNA.
DR RefSeq; WP_011873254.1; NZ_PDBV01000001.1.
DR AlphaFoldDB; A4F8Q7; -.
DR STRING; 405948.SACE_1100; -.
DR MEROPS; S16.012; -.
DR KEGG; sen:SACE_1100; -.
DR eggNOG; COG3480; Bacteria.
DR HOGENOM; CLU_042037_1_0_11; -.
DR Proteomes; UP000006728; Chromosome.
DR Proteomes; UP000225825; 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:UP000006728};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 128..171
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 226..324
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 231
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 276
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 333 AA; 34626 MW; A6E4700897B78324 CRC64;
MTSVLLVVVF GMLGAFVQVP FVALGPGPTY DTLGTEGDTP VIRIDGQQTY PTGGHLNMTT
VTVTDQLSLF GALGLWVSGR YALAPREVYF PPDKSEQQIE QENTKAFNDS QTTAETAALR
YLGYPTKVLA GEIVKGSPAD GVIEPGDRLI SANGRPVTDA ASLREALAAN RPGDRVEIRF
RHADEPERAA TVQLGQHPHG EPQGFLGVAA TERPDVPFGI EISLADVGGP SAGLMFSLAI
IDKLTPGEIN GGQFVAGTGE IDPAGTVGAI GGIPFKMVKA REAGATTFLV PAGNCAEAKA
QAPAGLRLAK VATLDEANKA LEALRNGQVP AGC
//
