ID   A0A117NUQ2_9ACTN        Unreviewed;       455 AA.
AC   A0A117NUQ2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Serine protease {ECO:0000313|EMBL:KUM67714.1};
GN   ORFNames=AQI70_35220 {ECO:0000313|EMBL:KUM67714.1};
OS   Streptomyces curacoi.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=146536 {ECO:0000313|EMBL:KUM67714.1, ECO:0000313|Proteomes:UP000054024};
RN   [1] {ECO:0000313|EMBL:KUM67714.1, ECO:0000313|Proteomes:UP000054024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40107 {ECO:0000313|EMBL:KUM67714.1,
RC   ECO:0000313|Proteomes:UP000054024};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces curacoi DSM 40107, type strain for
RT   the species Streptomyces curacoi.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC       Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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:KUM67714.1}.
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DR   EMBL; LMWJ01000034; KUM67714.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A117NUQ2; -.
DR   STRING; 146536.AQI70_35220; -.
DR   OrthoDB; 9798386at2; -.
DR   Proteomes; UP000054024; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR023834; T7SS_pept_S8A_mycosin.
DR   NCBIfam; TIGR03921; T7SS_mycosin; 1.
DR   PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR   PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000054024};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..455
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007152336"
FT   TRANSMEM        368..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          58..312
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   REGION          91..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          324..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          391..455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..447
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        67
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        100
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        261
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   455 AA;  46629 MW;  A55DF87FC202B799 CRC64;
     MRSKELVVKR FWSTTGVVAL TGALLLTSAP TASADYVRDK QWVIDVINFK KVWAESQGEG
     VTVAVVDTGV DGSHPDLTGQ VLKGMDVTGS GDAQNDTNGH GTGMASLIAG HGHGTNNSEG
     VIGLAPKAKI LPIKASSTGD DYRDDQWAEG VRYAVDQGAD VINLSFGGSS TSPDPEATEA
     IKYALQHNVV VVSGTGNDGT AGLEYPAKLP GVVAVGAVDE SLKVWKNSNF GPGVTLTAPG
     VNIARADTSE ASGYAEGSGV SDATAYVSAA AALVRAKYPD LTAGQVINRL IKSATFLDHD
     VKKVPDEEYG YGIIRPYAAL TRDIPKGPKQ GPLAQSAPST STNSGTASDD DSTSQAKKKK
     KKSSSGSILL IAGIAAVVVV IGIAAVVIRS RRNGGNGGPG SGGGTPPAGT GYPPQPPTGY
     QPYPNTPPSQ GYPAPPGQSP QHPNPYAQQP PHQGQ
//