ID E4MZW5_KITSK Unreviewed; 393 AA.
AC E4MZW5;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Putative serine endopeptidase {ECO:0000313|EMBL:BAJ30049.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:BAJ30049.1};
GN OrderedLocusNames=KSE_42640 {ECO:0000313|EMBL:BAJ30049.1};
OS Kitasatospora setae (strain ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304
OS / NBRC 14216 / KM-6054) (Streptomyces setae).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=452652 {ECO:0000313|EMBL:BAJ30049.1, ECO:0000313|Proteomes:UP000007076};
RN [1] {ECO:0000313|EMBL:BAJ30049.1, ECO:0000313|Proteomes:UP000007076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304 / NBRC 14216 /
RC KM-6054 {ECO:0000313|Proteomes:UP000007076};
RX PubMed=21059706; DOI=10.1093/dnares/dsq026;
RA Ichikawa N., Oguchi A., Ikeda H., Ishikawa J., Kitani S., Watanabe Y.,
RA Nakamura S., Katano Y., Kishi E., Sasagawa M., Ankai A., Fukui S.,
RA Hashimoto Y., Kamata S., Otoguro M., Tanikawa S., Nihira T., Horinouchi S.,
RA Ohnishi Y., Hayakawa M., Kuzuyama T., Arisawa A., Nomoto F., Miura H.,
RA Takahashi Y., Fujita N.;
RT "Genome sequence of Kitasatospora setae NBRC 14216T: an evolutionary
RT snapshot of the family Streptomycetaceae.";
RL DNA Res. 17:393-406(2010).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; AP010968; BAJ30049.1; -; Genomic_DNA.
DR RefSeq; WP_014137351.1; NC_016109.1.
DR AlphaFoldDB; E4MZW5; -.
DR STRING; 452652.KSE_42640; -.
DR KEGG; ksk:KSE_42640; -.
DR PATRIC; fig|452652.3.peg.4258; -.
DR eggNOG; COG4934; Bacteria.
DR HOGENOM; CLU_012501_3_0_11; -.
DR Proteomes; UP000007076; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR030400; Sedolisin_dom.
DR PANTHER; PTHR14218:SF42; PEPTIDASE S53 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51695; SEDOLISIN; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:BAJ30049.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007076};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..393
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003186263"
FT DOMAIN 65..393
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
SQ SEQUENCE 393 AA; 39348 MW; 31FC1F703307FF61 CRC64;
MHRPLALTAA LLTTSALTTA TLTSAHPAQA GPRWVHTCTA PARADTASCD ALRVVGAAAA
ADSDGYGPAE LRAAYGLPAD GGAGAVIAVV DAYDHPRAEA DLDVYRKHYG LPACTADSGC
FRKTDQRGGT RLPRGNTAWA GEIALDLAMV SAVAPRARIV LVEADSAAVG NLGAAVNTAV
ALGAQYVSIS WGTAENGNAA NYDSRYFDHP GTLIAAASGD GGYGVNFPAS SPHVLAVGGT
TLRPDGSARG WAETAWATSP TEGTASGCSG QLPKPAWQTD PGCDHRTVAD VAAVADPETG
VAVYQSYGGN GWYTYGGTSA AAPLVAAAAA LAGPVPAGSR PESFPYRHPD ALHDVTSGTT
ATDCAPAYLC AAGAGYDGPT GLGSPAGVAA FRP
//