ID B1KQU3_SHEWM Unreviewed; 607 AA.
AC B1KQU3;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Peptidase S8 and S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:ACA87699.1};
DE Flags: Precursor;
GN OrderedLocusNames=Swoo_3431 {ECO:0000313|EMBL:ACA87699.1};
OS Shewanella woodyi (strain ATCC 51908 / MS32).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=392500 {ECO:0000313|EMBL:ACA87699.1, ECO:0000313|Proteomes:UP000002168};
RN [1] {ECO:0000313|EMBL:ACA87699.1, ECO:0000313|Proteomes:UP000002168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51908 / MS32 {ECO:0000313|Proteomes:UP000002168};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella woodyi ATCC 51908.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; CP000961; ACA87699.1; -; Genomic_DNA.
DR RefSeq; WP_012326034.1; NC_010506.1.
DR AlphaFoldDB; B1KQU3; -.
DR STRING; 392500.Swoo_3431; -.
DR KEGG; swd:Swoo_3431; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_011263_15_3_6; -.
DR Proteomes; UP000002168; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07477; Peptidases_S8_Subtilisin_subset; 1.
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 InterPro; IPR034202; Subtilisin_Carlsberg-like.
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}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000002168};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..607
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002765134"
FT DOMAIN 126..323
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 365..431
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 432..502
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 134
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 167
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 454
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 607 AA; 61255 MW; 10B6F8E3245680ED CRC64;
MKLSKIAGAI IALTVSVSTT ATADDNRYII QVDNGNKGVV KALANRLGAE IHLDGNGFIS
ATFAGKDLSQ VKGLLNNPHI KLVEADQRRH LMSAYSDDAG NPMTQQVTPY AVYQSQADQV
AFNASAGMKV CVIDSGLDAS NTDFEWNNIS GDNDSGTGNW NENGGPHGTH VAGTIGAADN
SVGVVGMAPG VDMHIIKVFN ADGWGYSSDL AHAADLCSAA GANIISMSLG GGGSNSTESN
AFQSFVDAGG LVVAAAGNDG NNVRSYPAGY PSVMMIGAND ADNNIADFSQ FPSCTSGRGK
RATTDETICV EVTAGGVDTL STYPAGMATA SNMSADGAAY ASSAMENSGA IAGGTYYMGT
AEATDSGANG NICVIDRGVI SFHDKVANCE SSGGVGAVII NNEAGMLFGT LGDTNTTTIP
AVGAAFEDRA AIVAASNISI DIGTSDYGFM SGTSMATPAV SGVAALVWSN HNQCTGSEIR
EALKATAMDS GAAGNDVYFG YGIVKAAAAD AYLTANGCAG DGGGEPGGDF ALTADGYKSK
GVKKVDLTVN GAAGSNVDLY RDGSKIATTS ASSTYTDTIS GKGGGTFTYK ACDEGTTTCT
AEQTVVF
//
