ID B8CQS5_SHEPW Unreviewed; 1657 AA.
AC B8CQS5;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Serine protease, subtilase family {ECO:0000313|EMBL:ACJ30541.1};
GN OrderedLocusNames=swp_3864 {ECO:0000313|EMBL:ACJ30541.1};
OS Shewanella piezotolerans (strain WP3 / JCM 13877).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=225849 {ECO:0000313|EMBL:ACJ30541.1, ECO:0000313|Proteomes:UP000000753};
RN [1] {ECO:0000313|EMBL:ACJ30541.1, ECO:0000313|Proteomes:UP000000753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP3 / JCM 13877 {ECO:0000313|Proteomes:UP000000753};
RX PubMed=18398463; DOI=10.1371/journal.pone.0001937;
RA Wang F., Wang J., Jian H., Zhang B., Li S., Wang F., Zeng X., Gao L.,
RA Bartlett D.H., Yu J., Hu S., Xiao X.;
RT "Environmental adaptation: genomic analysis of the piezotolerant and
RT psychrotolerant deep-sea iron reducing bacterium Shewanella piezotolerans
RT WP3.";
RL PLoS ONE 3:E1937-E1937(2008).
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; CP000472; ACJ30541.1; -; Genomic_DNA.
DR RefSeq; WP_020913883.1; NC_011566.1.
DR STRING; 225849.swp_3864; -.
DR KEGG; swp:swp_3864; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_003205_0_0_6; -.
DR OrthoDB; 614750at2; -.
DR Proteomes; UP000000753; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02120; PA_subtilisin_like; 1.
DR CDD; cd04852; Peptidases_S8_3; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR046450; PA_dom_sf.
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; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034197; Peptidases_S8_3.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR017311; Sama-2696.
DR InterPro; IPR045051; SBT.
DR PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR PANTHER; PTHR10795:SF468; SUBTILISIN-LIKE PROTEASE SBT3.18; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PIRSF; PIRSF037895; Subtilisin_rel_Sama_2696; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52025; PA domain; 1.
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1657
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002866922"
FT DOMAIN 94..212
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 237..742
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 521..611
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT REGION 312..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1609..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 246
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 334
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 706
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1657 AA; 177220 MW; 0ADB0A1D89EA8227 CRC64;
MKLKKISLMT IAAIYAAGAG SVAASGNDNN NMRSIEITDA IIKYNEELRS GNSRAGNTVN
RPASNTQNIH RAIATNQNSK VPFKHQAGLQ GEQTYIVELS DKPVSLYRGG VEQFKATSPT
VNAVPSMLSP RGHNKLDTKS SSVKQYSQYL TGKQDQILNQ ISAKVGANLD IKNRYTLAFN
GMALRMTQEQ AANVANLPGI RNVSLEKVYE LHTDNGPGHI GADSIWTGSA ADDKYKGEGI
VVGVLDTGIN SDHASFAAVA GDGYTHKMPD RYSSYLGDCE KVEFASMCND KLIGVRSYES
ITESYMDAAF QPDQPSWNIT EPKRPQNGED YNGHGSHTAS TAAGNELFNV EHVVAVTGET
GDGLGTGLVF DKVSGVAPRA NIIMYQVCFP GDGSYGDNYG GCPGSALLAG IEDAVADGVD
VINYSIGSPF GTFPWDDPME MGFLAAREAG ISVSASAGNS YAPQYASQAR GAIDHFSPWI
TSVAATTHGR EIAVEGKTLT NATGGEQPLE LVGGGITGAY TGPVVEAKAY GSEFEKCNDP
FPADFFSVDP DGNPFATAPI VVCKRGDIAR VAKATNVEAG GAGGFILWNS GYAETIANDP
FSIPGIQIDY GSYYGNYQNG YFGLQDWLAA GDNHSITITA SEVVANERDA DYVADFSSRG
PNLEAPDVMS PNLAAPGVDV FAAWADEMPF SMQGMPADYA AISGTSMAAP HVAGAMALLT
QAHPDWTPAE IQSALMTTAS LDSATRSRDS SPYDPVPAGY SDAGSGVINV ARANNAGLLL
SETAENYRAA NPNNGGNIHT LNLPYFYQDN CAGSCSWMRT VTATEDGTWT VDATANIMDG
APMLELEVSP KTFTLKAGES QSISLKAKVL EVEAIGADSS GLQLTGSVKL TPANSSSPMQ
HLPVGVRYSG DNLPPEVSGI IHREQGHTLT PMLNTDEIQS LNSKVFGLTK GETFTYALPR
AEARLYSDGL TVEEIEADGG AKVHFFDVPA GTQRIVWEVL SAPKHAYTSI DLGMDINEDG
DIQWLDEAIC YSFTDNGDFC AINNPAPGRY WAIAANWKYD FEDPKNLADE FVLSLGIVGE
SDDANMTVEG PATTDGMTPY QLQLNYNLPG ATDGDTYYGV VALGSDDYNA TNLGDFAVKL
QHMGADTEIT ASQTAAKVGD VVNYVVDLAP NLVGAEREFT LNATISEGMQ LIEDSIVVGG
VGDYEAGLTV NGNAISISAA QASSSDMKRH YVYTTNLDDA TCKVPYGDDE TFYDLPMQGY
QDLGISGLSN QMLYIPMEEN GLPHIPLYAN PERFAQNTLG ISPFGYIQLD QNPEFWNYNQ
PFTDMFQTFP DTVIAPLWRG DVQMPQGSID WATFRYINVV YGVVTNDHYI FQWDGGEEWN
SFLVGNTNPD PDAKFNIQTI ISNSISFDPE TPEMIFAYKT LKSANDHFGS IGLHGYWGER
TPFGPLSGYF NDGFAFNDVD EKVSEGTVVC ADYRGPEQTA LSLKFSARVS AAAIGSDNVV
SVDTQYADSE LVSVSHTLST PTNITVAAMS DMVMEENSTI EGLTVMYNDV KGTVNGMTVT
GDYITAVVTG ETFAITPDTD WHGTTEVTVT VHDMAYPSDQ GSTSFMLTVN SDGVEPTPPP
AEEPPVEEES NDSSGGSLGF LALALLGLVA SSRKKRH
//