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Database: UniProt
Entry: A0A1S1MNT9_9GAMM
LinkDB: A0A1S1MNT9_9GAMM
Original site: A0A1S1MNT9_9GAMM 
ID   A0A1S1MNT9_9GAMM        Unreviewed;       601 AA.
AC   A0A1S1MNT9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Peptidase S8 {ECO:0000313|EMBL:OHU90076.1};
GN   ORFNames=BET10_14980 {ECO:0000313|EMBL:OHU90076.1};
OS   Pseudoalteromonas amylolytica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1859457 {ECO:0000313|EMBL:OHU90076.1, ECO:0000313|Proteomes:UP000179786};
RN   [1] {ECO:0000313|EMBL:OHU90076.1, ECO:0000313|Proteomes:UP000179786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JW1 {ECO:0000313|EMBL:OHU90076.1,
RC   ECO:0000313|Proteomes:UP000179786};
RA   Wu Y.-H., Cheng H., Jin X.-B., Wang C.-S., Xu X.-W.;
RT   "Pseudoalteromonas amylolytica sp. nov., isolated from the surface
RT   seawater.";
RL   Submitted (SEP-2016) 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:OHU90076.1}.
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DR   EMBL; MKJU01000027; OHU90076.1; -; Genomic_DNA.
DR   RefSeq; WP_070986044.1; NZ_MKJU01000027.1.
DR   AlphaFoldDB; A0A1S1MNT9; -.
DR   STRING; 1859457.BET10_14980; -.
DR   OrthoDB; 9790784at2; -.
DR   Proteomes; UP000179786; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR034182; Kexin/furin.
DR   InterPro; IPR002884; P_dom.
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; PTHR42884:SF32; EXTRACELLULAR SERINE PROTEASE; 1.
DR   PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51829; P_HOMO_B; 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..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..601
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010207575"
FT   DOMAIN          451..601
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   ACT_SITE        82
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        116
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        355
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   601 AA;  64482 MW;  5140F2939CE95CDE CRC64;
     MNNNKSLLAL AVVAATGSVY ANTSPDQDLI KRDPLTFQQW HLQNTGQTGF SLSAGKVGED
     LNLDFADRMG IKGRGITVSV IDTGVEISHP DLKNNVVPGS RNLIDGSDYP VDTHGHGTAV
     AGLIAAEEGN NLGGRGVAPY ANLIGFNYLS EQSLASWMVS HGLSEDFRVL DRFTDPRVFN
     QSYGSTPSSP PNGDLSLDPE YALVEQVMRD ISLDSHWGRG AAYVKSAGNS FRYYNTYIQG
     IPFYVIPYEN NEFFNNNGLP FHNANIELGN TLFWNLVVSS LNADGHLSSY SSAGANIFLS
     APGGEYGQDK PAMVTVDLTG CEQGMNVTGI HKNALHGGSQ LDPNCDFTGV MNGTSSAGPN
     VAGAVATVMS ANPALDARTV RHILASTARK VDPQHQGVSL DFETASGETV TYDAVPGWQT
     NAAGYHFHSF YGLGAVNVDD AVYKALFTGA SLPQLQITPW QKQTAGVTVP DASLVGAQST
     MGIDQNLTIE AVQLKLNLDH ERLRDIAIEL TSPSGTRSVM MSARTGFLDG TDGGYTDTVM
     LSHQFYGEKS QGNWTLKVLD TDKGTSSTLI YNPEIGLFAT NRTNNTVDGV LKDWSLRIYG
     H
//
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