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Database: UniProt
Entry: A0A136I1D8_9ALTE
LinkDB: A0A136I1D8_9ALTE
Original site: A0A136I1D8_9ALTE 
ID   A0A136I1D8_9ALTE        Unreviewed;       617 AA.
AC   A0A136I1D8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Alkaline serine protease {ECO:0000313|EMBL:KXJ61419.1};
GN   ORFNames=AXW14_09300 {ECO:0000313|EMBL:KXJ61419.1};
OS   Alteromonas sp. Nap_26.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=1795869 {ECO:0000313|EMBL:KXJ61419.1, ECO:0000313|Proteomes:UP000070342};
RN   [1] {ECO:0000313|Proteomes:UP000070342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Donaho J.A., Gutierrez T., Seitz K.W., Teske A.P.,
RA   Baker B.J.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC       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:KXJ61419.1}.
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DR   EMBL; LSMP01000080; KXJ61419.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136I1D8; -.
DR   Proteomes; UP000070342; 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; 3.50.30.30; -; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR003137; PA_domain.
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; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF00082; Peptidase_S8; 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..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..617
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007472587"
FT   DOMAIN          127..325
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          368..431
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          438..503
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        135
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        168
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        455
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   617 AA;  62330 MW;  2062F8AC59EF5E0A CRC64;
     MNNKKFTPSL IAAGLALSSF GALADNDRYI IQVDNNAKGI VKALAKQSGA QIHVDADGFI
     AATFNGKTLS DVKGLLNNPH VKLVEADQKR APMALYSDDA GDPTQTQLTP YAVYQSQADQ
     VTFDSNAGMK VCVIDSGLDS SNADFNWSAI TGDNDSGTGN WFENGGPHGT HVAGTIGAAD
     NGFGVVGMAP GVDMHIIKVF NAAGWGYSSD LAHAAQLCSQ AGANIINMSL GGGGANSTEE
     NAFKDFVAAG GLVVAAAGND GNSVRSYPAG YSSVMMIGAN DADNNIADFS QYPSCTSGRG
     KRVTTDETIC VEVTAGGVDT LSTYPAGGAS MSTLSADGIG FASSAMENTG NASAQTYFFG
     LGDSVDSGAA GKVCVIDRGS ISFYDKVNNC ELSGGVGAVI INNEAGMLYG TLGDTNNTSI
     PAVGAALEDR SALIAASTVD ISIGASDYGF MSGTSMATPA VAGIAALVWS NHPTCSGEEI
     RSALKATALD AGAAGKDDFF GYGIAQAADM NDYLTQNGCA GGNGGGDNGG GDTGGGTGDL
     TLSATGYKVK GAQTVDLTWS DATSSNVDIY RDGNVITTTA NDGTYTDALN VKGGGSYTYQ
     VCEAGTTTCS ATVSVVF
//
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