ID B2FI22_STRMK Unreviewed; 1118 AA.
AC B2FI22;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Extracellular serine protease {ECO:0000313|EMBL:CAQ47536.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:CAQ47536.1};
GN OrderedLocusNames=Smlt4145 {ECO:0000313|EMBL:CAQ47536.1};
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ47536.1, ECO:0000313|Proteomes:UP000008840};
RN [1] {ECO:0000313|EMBL:CAQ47536.1, ECO:0000313|Proteomes:UP000008840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a {ECO:0000313|EMBL:CAQ47536.1,
RC ECO:0000313|Proteomes:UP000008840};
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(2008).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
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DR EMBL; AM743169; CAQ47536.1; -; Genomic_DNA.
DR RefSeq; WP_012481342.1; NC_010943.1.
DR AlphaFoldDB; B2FI22; -.
DR MEROPS; S08.162; -.
DR EnsemblBacteria; CAQ47536; CAQ47536; Smlt4145.
DR KEGG; sml:Smlt4145; -.
DR PATRIC; fig|522373.3.peg.3917; -.
DR eggNOG; COG1404; Bacteria.
DR eggNOG; COG4625; Bacteria.
DR HOGENOM; CLU_005887_2_0_6; -.
DR Proteomes; UP000008840; Chromosome.
DR GO; GO:0019867; C:outer membrane; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04848; Peptidases_S8_Autotransporter_serine_protease_like; 1.
DR Gene3D; 2.40.128.130; Autotransporter beta-domain; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR005546; Autotransporte_beta.
DR InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR InterPro; IPR006315; OM_autotransptr_brl_dom.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034061; Peptidases_S8_Autotransporter.
DR NCBIfam; TIGR01414; autotrans_barl; 1.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF03797; Autotransporter; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00869; Autotransporter; 1.
DR SUPFAM; SSF103515; Autotransporter; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51208; AUTOTRANSPORTER; 1.
DR PROSITE; PS51892; SUBTILASE; 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:UP000008840};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..1118
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002776258"
FT DOMAIN 839..1118
FT /note="Autotransporter"
FT /evidence="ECO:0000259|PROSITE:PS51208"
FT ACT_SITE 123
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 200
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 435
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1118 AA; 116012 MW; 8317C7264647CC80 CRC64;
MNHPLHGRSS HSRSPLHSRL ALAVSSSLLL AAAAPAMAGE ALDAWQQQRQ LQAAWAQPAV
SAPAASTAAT PAATGTALLG NPGDAASWRS DEFNADWGLG AMGADYAYAR GLTGKGVRLA
LFDTGSALAH PEFAGRNTSS ITIGPNCASP GTVGGTGACS QTQGDQPGIN YYTLGAGVPA
SLQANIIAAG REWGFRYADH GTHVLGTIGA NRNGTGMHGV AFGADLTTAR VFGDTYYEWR
RQASGGYLPE AVERTDPDGA ARLDMYAQLQ AQGVRAINHS WGISTRNMTV AALDAQYARI
GAGYDVYGSI YKDSANAPAS QLIQVWSAGN GSGAVAGITA ALPRWKPEIE PYWLAVANVR
QPNTANGETD YVINAGSSIC GAAANWCISA PGTAILSTIV SGDIQGRLEK TADYVRLLID
SQNPTYDYGL KTGTSMAAPH ITGALGLLME RFPYLDNAQV RDVLLTTARD LGAAGVDPIY
GWGMIDLRRA IEGYGSLRVD TNVVMNQRAG GLKVWEGDAW DDWTNDIGGP GTLTKSGIGW
LRLSGDNSFN GAVLREGTLE LNGSNTLTSA VDVQGGRFLL NGSLVSTALT TTGGVSTVSA
SGVLKDGNLT VNGGVVSFNG MQTGGTTTVG SNGLLKGIGT LGSTRVDGTI APGNSIGTLT
INGDYVQGAT GVYAAELAPG GRSDQLHVTG TATLGGTLVA LPEPGIYYLG EQFNFIRADG
GINGQFAKTD FSAFSPFLQF SLAYGANGTR IDVARGASLA SAATTPNQRA VAAAADLLAI
NQGLPKPLTQ LFPQQVGGVL DGLSGELHAA TPLALVEGSR YVRDAALSRR AGAVAPGADA
GDATGAWVQA LGGNSRLDGN SNAARTEANS NGLLAGIDHE FSGWQVGVLA GTGRTDVKQQ
ALRAKSKIDN THFGAYASHN WGGLGLRGGV AWSKHKVKST RDVDFAGFSD SLSARYNAHT
RQAFIEAGYR FGGPEAGLES YLQVARVEVD LKPINERGGA AALHGKVDDT GTTIATAGLR
FDKGLKASFQ QDSWLHLRGG VGYRRASGDR SQLADLAFAN SSTTFAVEGA PIADSAVVAE
LGLSAWLTPR QQLELGYSGQ YGSESRDHSA NMRWSVRF
//
