ID A0A1D7VR77_9ACTN Unreviewed; 272 AA.
AC A0A1D7VR77;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Lon proteolytic domain-containing protein {ECO:0000259|Pfam:PF05362};
GN ORFNames=SL103_26250 {ECO:0000313|EMBL:AOP49280.1};
OS Streptomyces lydicus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=47763 {ECO:0000313|EMBL:AOP49280.1, ECO:0000313|Proteomes:UP000094094};
RN [1] {ECO:0000313|EMBL:AOP49280.1, ECO:0000313|Proteomes:UP000094094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=103 {ECO:0000313|EMBL:AOP49280.1,
RC ECO:0000313|Proteomes:UP000094094};
RA Jia N., Ding M.-Z., Gao F., Yuan Y.-J.;
RT "Complete genome sequencing of Streptomyces lydicus 103 and metabolic
RT pathways analysis of antibiotic biosynthesis.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP017157; AOP49280.1; -; Genomic_DNA.
DR RefSeq; WP_069571394.1; NZ_CP017157.1.
DR AlphaFoldDB; A0A1D7VR77; -.
DR KEGG; slc:SL103_26250; -.
DR OrthoDB; 2356897at2; -.
DR Proteomes; UP000094094; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
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 SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000094094};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 165..246
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|Pfam:PF05362"
SQ SEQUENCE 272 AA; 27932 MW; 65E43C020F594A4C CRC64;
MTTRPSPDPS PRPRLLARPR ALALGAVPAV ALLAVAAFAP LPYSVARPGQ TTDVLGVYRG
TEVISVSGAP VRRTSGQLRM AAIRATGPHV GASLSELADG WFRTDRAVMP REAVFPSGKS
DEAVARHNTT EMKSSQRAAT SAALRLLKQD PRRVRVRLTL DDVGGPSAGL MFSLGIVDKL
AGDGSGGDLT GGRTIAGTGT IDADGTVGPV GGAALKTRAA ERDGASVFLV PKAECAQLQP
APDGLRLVPV TTLRDAVHAL RALAGGGRVP SC
//
