ID B2FQ06_STRMK Unreviewed; 580 AA.
AC B2FQ06;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Secreted serine protease {ECO:0000313|EMBL:CAQ44436.1};
GN Name=expR {ECO:0000313|EMBL:CAQ44436.1};
GN Synonyms=StmPr1 {ECO:0000313|EMBL:CAQ44436.1};
GN OrderedLocusNames=Smlt0861 {ECO:0000313|EMBL:CAQ44436.1};
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ44436.1, ECO:0000313|Proteomes:UP000008840};
RN [1] {ECO:0000313|EMBL:CAQ44436.1, ECO:0000313|Proteomes:UP000008840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a {ECO:0000313|EMBL:CAQ44436.1,
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.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; AM743169; CAQ44436.1; -; Genomic_DNA.
DR RefSeq; WP_005408178.1; NC_010943.1.
DR AlphaFoldDB; B2FQ06; -.
DR MEROPS; S08.110; -.
DR EnsemblBacteria; CAQ44436; CAQ44436; Smlt0861.
DR GeneID; 61464771; -.
DR KEGG; sml:Smlt0861; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_011263_8_2_6; -.
DR Proteomes; UP000008840; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07496; Peptidases_S8_13; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
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; IPR034176; Peptidases_S8_13.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF04151; PPC; 1.
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}; 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..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..580
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002777523"
FT DOMAIN 168..457
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 501..566
FT /note="Peptidase C-terminal archaeal/bacterial"
FT /evidence="ECO:0000259|Pfam:PF04151"
FT ACT_SITE 177
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 237
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 409
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 580 AA; 58291 MW; C462845BA576C3C7 CRC64;
MSQVTQPRVR RVWVVLGASV LSSLLLATPA LAGDVQLSGL QSAPTHQRFI VKYRDGSAAV
ANTTALASSL KTAAAGLASS QGRALGLQQV RKLAVGPTLV KTDRPLDQAE SELLMRKLAA
DPNVEYVEVD QIMRATLTPN DTRFSEQWGF GTSNAGINIR PAWDKATGTG VVVAVIDTGI
TNHADLNANI LPGYDFISDA AMARDGGGRD NNPNDEGDWY GANECGSGIP ASNSSWHGTH
VAGTVAAVTN NSTGVAGTAF NAKVVPVRVL GKCGGYTSDI ADAIVWASGG TVSGVPANAN
PAEVINLSLG GGGSCSTTYQ NAINGAVGRG TTVVVAAGNS NTNVSSSVPA NCPNVIAVAA
TTSAGARASF SNYGTGIDIS APGQSILSTL NTGTTTPGSA TYASYNGTSM AAPHVAGVVA
LMQSVAPSPL SPAQVESIIK STARPLPGAC SGGCGAGIID ANAAVAAAIN GGGNPNPGGN
VLQNNVPVTG LGAATGAELN YTVAVPAGST QLRVAISGGS GDADLYVRQG SAPTDTTYTC
RPYLSGNSET CTINSPAAGT WYVRVKAYST FSGLTLNAQY
//
