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Database: UniProt
Entry: A0A1E7K0S8_9ACTN
LinkDB: A0A1E7K0S8_9ACTN
Original site: A0A1E7K0S8_9ACTN 
ID   A0A1E7K0S8_9ACTN        Unreviewed;       439 AA.
AC   A0A1E7K0S8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Peptidase S41 {ECO:0000313|EMBL:OEU97534.1};
GN   ORFNames=AN217_06245 {ECO:0000313|EMBL:OEU97534.1};
OS   Streptomyces qinglanensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=943816 {ECO:0000313|EMBL:OEU97534.1, ECO:0000313|Proteomes:UP000175829};
RN   [1] {ECO:0000313|EMBL:OEU97534.1, ECO:0000313|Proteomes:UP000175829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCSIO M10379 {ECO:0000313|EMBL:OEU97534.1,
RC   ECO:0000313|Proteomes:UP000175829};
RX   PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA   Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA   Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT   "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT   Adaptation to the Marine Environment and Their Diversity at the Genomic
RT   Level.";
RL   Front. Microbiol. 7:998-998(2016).
CC   -!- SIMILARITY: Belongs to the peptidase S41A family.
CC       {ECO:0000256|ARBA:ARBA00009179}.
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:OEU97534.1}.
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DR   EMBL; LJGV01000022; OEU97534.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E7K0S8; -.
DR   PATRIC; fig|943816.4.peg.606; -.
DR   Proteomes; UP000175829; Unassembled WGS sequence.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07560; Peptidase_S41_CPP; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR004447; Peptidase_S41A.
DR   InterPro; IPR005151; Tail-specific_protease.
DR   PANTHER; PTHR32060:SF22; CARBOXYL-TERMINAL-PROCESSING PEPTIDASE 2, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF03572; Peptidase_S41; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00245; TSPc; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW   Protease {ECO:0000256|ARBA:ARBA00022825};
KW   Reference proteome {ECO:0000313|Proteomes:UP000175829};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT   DOMAIN          150..206
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          47..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          127..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   439 AA;  45141 MW;  B6AB3CDF287B1E95 CRC64;
     MPGSWFLETR PRRPRRGALT MVFAGVLATG AATGAFGGEL AAFGTAAPGS AAHGAGRSAL
     GGPADAKGES AGSRGARGRT GGDAADAVVS RSGDRWSAAY SAREYEGLRQ ALDGSYVGVG
     ISVRQTRADA PRTDGPGSGA ADAESATDRA GGQRAGRGTA VRVERVQPGS PADRAGIRAG
     DRLRSVAGRH VTGKPVTAVV ALLRGSDPDS PADAADPGTR VRLHLTRGGR DLHRTLRRER
     LTTESVRVDQ VGDGVTRVAI RSFTRGSGEQ VRKAVRERVP ETGPVLLDLR GNSGGLVDEA
     VTAAGAFLDG GLVATYDDDG TEHALYAEDD ADQPGDVERR PLVVLVDGGT MSAAEMLTGA
     LQDRGRAVVV GSRTFGKGSV QMPRPQSDGS VAELTVGHYT TPSGRDVEGH GIAPDLSVRS
     RGESMERART VLSGLGARS
//
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