ID A0A0F4JT14_9ACTN Unreviewed; 1111 AA.
AC A0A0F4JT14;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:KJY37325.1};
GN ORFNames=VR44_06000 {ECO:0000313|EMBL:KJY37325.1};
OS Streptomyces katrae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68223 {ECO:0000313|EMBL:KJY37325.1, ECO:0000313|Proteomes:UP000033551};
RN [1] {ECO:0000313|EMBL:KJY37325.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL ISP-5550 {ECO:0000313|EMBL:KJY37325.1};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-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:KJY37325.1}.
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DR EMBL; JZWV01000110; KJY37325.1; -; Genomic_DNA.
DR RefSeq; WP_045946321.1; NZ_JZWV01000110.1.
DR AlphaFoldDB; A0A0F4JT14; -.
DR STRING; 68223.GCA_002028425_02512; -.
DR PATRIC; fig|68223.7.peg.2414; -.
DR eggNOG; COG1404; Bacteria.
DR OrthoDB; 9813435at2; -.
DR Proteomes; UP000033551; 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; 2.
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; 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; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 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..41
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 42..1111
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002470854"
FT DOMAIN 203..641
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 962..1025
FT /note="Peptidase C-terminal archaeal/bacterial"
FT /evidence="ECO:0000259|Pfam:PF04151"
FT REGION 42..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..184
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 394
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 590
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1111 AA; 115464 MW; C66A2F095FDBE639 CRC64;
MTLESPSSTG AIPGARRAAR VAAAAGLVAA LCATGAVPVF AATGDTNPSA PAPAKSADQK
LGSADAELLQ EAKAKGDATV TVMVATAPGQ TKQVSDQLHA VQGASVGQTY DKLGYVRATL
PTDKAEAALK AAAKLESVHG MDLKQEIQLP DPRPDSGKDG SGQKTASETY PGPDKNTPAK
NPYNPSFETG AVDFVAKNPQ ADGRGVTIGI LDSGVDIAHP ALQKTTTGER KIVDWVTATD
PILDNDATWR PQVTPVTSAG GTFTAGGQSW KAPEGTFQWS RFSESITANG DMKGDVNRDG
DTTDKFGMLY DPVAGTVRVD TDQDGDFTNN EPMKPYKDGY QIGYFGTDNP ATDVAERIPF
VIQIRKDVPM DPFGGDWVGK KADFVNIGII ESEHGTHVAG ITAANSLFGG KMNGEAPGAK
IVSSRACSWS GGCTNIALTE GMIDLVVNRG VDIVNMSIGG LPALNDGNNA RSELYKNLID
TYGVQLVISA GNEGPGVNTI GDPGLADKVI SVGAAVSKET WAANYGSGVT KKYNMFPFSS
RGPREDGGFT PTITAPGAAI NTTQTWLPGS PVKEAGYSLP AGYSMLQGTS MSSPQAAGAS
ALLISAAKQA KIALPPANLR VALTSTAKKI DDVPAHAQGS GLIDINKAWE SIQRGAKANE
FTVKAPVDTA LDQFLKTPGF GTGLYDREGG LKVGQKKVYD VVVTRTTGPK YGTRHNLSWR
NNDGTFKVVG GGGYDYVTLP LNKPVTIKVE ANVKSAGVHS GILQLDDPTT EGIDKQILAT
VVASTPLAQP SFALSDTSSV QRNSHKSYFV TVPQGAKTLE VALGGLAADS QTRFISIHPY
GTGVEDSATT QCYPNYNNPA NKCRPDLRSY DNPQPGVWEI EVESRRTSPL LDNPFKLDVS
VLGAGFDPAV KVLPEVKQGA PAPVQWTVNN TGAAISGGKL QGGPLGSAKV DKPTIAAGET
KTTEVTVGEG VSRLDVAINH TSDAAADLDL EVYKDGVKVA SSADGDSDES VSLDKPAAGT
YTVKVIGYAV PSGSTTYDYR DVYFSSALGT VQVDEAAAVN LATGASAQVS ANVLVSSAAP
EGRQFFGQVQ LLNGRGTAAG TGSVQIDKVT P
//
