ID A0A0S2JIB9_9GAMM Unreviewed; 1041 AA.
AC A0A0S2JIB9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:ALO35635.1};
GN ORFNames=CMT41_13625 {ECO:0000313|EMBL:ALO35635.1};
OS Colwellia sp. MT41.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=58049 {ECO:0000313|EMBL:ALO35635.1, ECO:0000313|Proteomes:UP000065319};
RN [1] {ECO:0000313|EMBL:ALO35635.1, ECO:0000313|Proteomes:UP000065319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MT41 {ECO:0000313|EMBL:ALO35635.1,
RC ECO:0000313|Proteomes:UP000065319};
RA Kyaw T.S., Ugalde J., Peoples L., Narasingarao P., Chastain R.A.,
RA Yayanos A., Methe B.A., Bartlett D.H.;
RT "Distinctive Gene and Protein Characteristics of Extremely Piezophilic
RT Colwellia.";
RL Submitted (NOV-2015) 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}.
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DR EMBL; CP013145; ALO35635.1; -; Genomic_DNA.
DR RefSeq; WP_058027565.1; NZ_CP013145.1.
DR AlphaFoldDB; A0A0S2JIB9; -.
DR STRING; 58049.CMT41_13625; -.
DR KEGG; com:CMT41_13625; -.
DR OrthoDB; 614750at2; -.
DR Proteomes; UP000065319; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04818; PA_subtilisin_1; 1.
DR CDD; cd04852; Peptidases_S8_3; 1.
DR Gene3D; 2.60.40.2310; -; 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; IPR045051; SBT.
DR InterPro; IPR041469; Subtilisin-like_FN3.
DR PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR PANTHER; PTHR10795:SF468; SUBTILISIN-LIKE PROTEASE SBT3.18; 1.
DR Pfam; PF17766; fn3_6; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 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}; Reference proteome {ECO:0000313|Proteomes:UP000065319};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1041
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006600290"
FT DOMAIN 100..151
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 179..655
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 436..522
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 711..817
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 188
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 262
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 602
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1041 AA; 108712 MW; B75BA6427C71890C CRC64;
MYFKKSIIGS LITLALTAGA SNAVVANEIT GDISKFKSVG SEINSKHKTT GYIIQLRGKT
GIAQAQDIGE LLPTNQLVAN TGNRYNAYTP AMKAYTQAME NKQKQVASSI DSLEILHSFK
HTYNGFTAKL NAKQKAQLES HPDVIGIWED KLHVVNTANT PEFLGLTGPG GQHALNIKGE
GVIIGVIDTG VWPENPSFAD DGSYSDPADL GWQGTCDTGT DLEFSCNNKL IGARYFGASF
SSQYDIQYSL GEFDSPRDAD GHGSHTASTA GGNEGVAAIL SGAPAGTVSG MAPRARIAVY
KVCWNSDYVS PEGNKERGCF GGDTMAAIDA AVTDGVDVIN YSIGGSRTDL TVPASAAMLN
AAAAGVFVAV SAGNSGPDKE TVGTPAPWVT SVAASTYNGT STIIGKALDV TSGSLAGTSL
MSVPAAFAPA TVGLAGELAL AEPVEACNDA PLTNADELVG KIALIARGSC AFTEKFINAQ
NAGAIGALVY TYDGTSPFSM GGEDPAVTIT GSMISFADGQ ALTASVLAES TAVIFTDTAA
SGEVVEVGNT IASFSSRGPN LNTYDIIKPD ITAPGVKILA ATTSAPMSGT QGETFMYLQG
TSMSSPHIAG LAALFKESNS SWTPAQIKSA MMTTARQDLT KEDGTTPADP YDFGSGHVAP
VSALDPGLLF DINLADYLAF LCGQDKESFV AGYDTSCADL TTKGFSTDAS QLNLPSIAIA
ELLEAETIFR TVSNATLAAS SYSATIEAPA GFDVSIQTFD ANGDETPTTS LDVDADGKAS
FALTFSKTET TEVNAWKFGA ITWTDSAGHS VRLPLAIKAV PTVKIEVPEL ISGDLRRGRF
RFPVKMLYSG RTSIKHAGLV APFGTAGTVE ADPAKEFEFL GAGTNYHMFH IPVGTQVARF
SLSDALVTEA DSDLDLYVYR CDKWSCTQVA NSLNAGSNEN VILTNPEPRA DVSVGDVYLT
MIHGYSTGAA SATDYTMVGW IADQAESTTR VISSRRAITG RFNYTTIMTR GLPTGTTYMG
AVTYFNADGE AEGTTVLELN N
//
