ID A0A0M8Z7Y0_9ACTN Unreviewed; 1098 AA.
AC A0A0M8Z7Y0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:KOX53290.1};
GN ORFNames=ADL09_01755 {ECO:0000313|EMBL:KOX53290.1};
OS Streptomyces sp. NRRL F-7442.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519498 {ECO:0000313|EMBL:KOX53290.1, ECO:0000313|Proteomes:UP000037772};
RN [1] {ECO:0000313|EMBL:KOX53290.1, ECO:0000313|Proteomes:UP000037772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-7442 {ECO:0000313|EMBL:KOX53290.1,
RC ECO:0000313|Proteomes:UP000037772};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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:KOX53290.1}.
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DR EMBL; LGEH01000001; KOX53290.1; -; Genomic_DNA.
DR RefSeq; WP_053662297.1; NZ_LGEH01000001.1.
DR AlphaFoldDB; A0A0M8Z7Y0; -.
DR PATRIC; fig|1519498.3.peg.360; -.
DR OrthoDB; 9813435at2; -.
DR Proteomes; UP000037772; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF04151; PPC; 2.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..40
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 41..1098
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005829886"
FT DOMAIN 203..631
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 793..870
FT /note="Peptidase C-terminal archaeal/bacterial"
FT /evidence="ECO:0000259|Pfam:PF04151"
FT DOMAIN 946..1014
FT /note="Peptidase C-terminal archaeal/bacterial"
FT /evidence="ECO:0000259|Pfam:PF04151"
FT REGION 40..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 212
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 387
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 583
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1098 AA; 113709 MW; A0A5ABE1362317D1 CRC64;
MTHTPQREPI PGVRRAARIV LATGLVAALA AVGPVPAALA ADGPASTTPP ADASVKSAHD
KLGSHDADLL AAAKAGGEKN VTMMVATAPG ATAQVAKELN AIAGGTVGRT YDELGYVRAT
VPTAKADSAI AAAAKLSSVH GIDLRDEIEL DDPTPSADMA EGAAHKGRSY PAPDRRTPAE
NPYNPSFETG AVDFVKKNPK SDGRGVTIGI LDSGVDLAHP ALQKTTTGER KIVDWVTATD
PVVDGDRTWR PMTTSVSGPV FTYGGQTWTA PAGSYRMSTF LESYTTGGDA AGDANRDGDT
TDSWGVLYDA EAGTVRVDLN NNHDFSDDTP MKPYKDGFQV GYFGTDDPKT DVAERQPFVV
EIRKDVVYNS AGAKADFVNI GVIESEHGTH VAGLAAAHGL FGGRMDGAAP GAKIVSSRAC
TWSGGCTNVA LTEGMIDLVV NRGVDIVNMS IGGLPALNDG NNARAELYTR LIDTYGVQLV
ISAGNSGPGA NTIGDPGLAD KVISVGASIS RETWAANYGS EVKTKYQMMP FSSRGPREDG
GFTPTLTAPG AAVNSIQTWM PGAPVPEAGY DLPAGYGMLQ GTSMASPQAA GASALLLSAA
KQARIDLTPA KLRTALTSTA DHIKGAQAYE EGAGLINIPD AWKSVRRGAT AHEYTVEAPV
DTAIDQFLKT PGHGTGLYDR EGGLKAGQKK TYEITLTRTS GADKAIRHEL HFENNAGNTF
RVVGSDEVKL PLNEPVTVRV EARPGSAGLK SAILEVDDPR TEGVDQQVLT TVVVSAPLTY
DFSAKGSVQR NSTASYFVTV PEGAKSLEVA IGGLKGRSQT RFISIHPYGV PADNTSTPYC
YNNYLDGNGC RPDVRAYADP QPGVWEVEVE ARRTSPLLDN PYKLDVTVLG AAFDPQVVTV
PEAKAGTPAD ASWTVTNKYA ALEGKLVGGP LGSSETSRPT IKQGQTATST VEVPEGAESL
DVAIGGVSDA AADLDLTVYG ENGAVVAQSA DGDSEESVSV AKPAAGTYTV VVAGYSVPSG
STEYDYRDVY FSAGLGSVTV DGSAAVKLGT GGSATVTGSV TALAAAPEGR EFFGRVQLVN
AHGTVAGLGS VRIGKVVP
//
