ID W8F0R2_9BACT Unreviewed; 522 AA.
AC W8F0R2;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Subtilisin-like serine protease {ECO:0000313|EMBL:AHJ97617.1};
GN ORFNames=Hsw_2022 {ECO:0000313|EMBL:AHJ97617.1};
OS Hymenobacter swuensis DY53.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1227739 {ECO:0000313|EMBL:AHJ97617.1, ECO:0000313|Proteomes:UP000019423};
RN [1] {ECO:0000313|EMBL:AHJ97617.1, ECO:0000313|Proteomes:UP000019423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY53 {ECO:0000313|EMBL:AHJ97617.1,
RC ECO:0000313|Proteomes:UP000019423};
RA Jung J.-H., Jeong S.-W., Joe M.-H., Cho y.-j., Kim M.-K., Lim S.-Y.;
RT "Complete genome sequence of ionizing-radiation resistance bacterium
RT Hymenobacter swuensis DY53.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
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DR EMBL; CP007145; AHJ97617.1; -; Genomic_DNA.
DR RefSeq; WP_044001992.1; NZ_CP007145.1.
DR AlphaFoldDB; W8F0R2; -.
DR STRING; 1227739.Hsw_2022; -.
DR KEGG; hsw:Hsw_2022; -.
DR PATRIC; fig|1227739.3.peg.2236; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_039707_0_0_10; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000019423; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00306; Peptidases_S8_S53; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51892; SUBTILASE; 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:UP000019423};
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..522
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004908105"
FT DOMAIN 231..509
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 240
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 292
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 463
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 522 AA; 55080 MW; CF13C1570A930B93 CRC64;
MRTLTLAPAA LLALALASCS QETTEQLPTP QPDPTTALSI QQLDEQILST LKQSTQYDWN
KASAHTVWSA LEQSDHVLSV GYQPAGLQGG AALPEDARQS PEWQQARAQV LALILAEEQK
TNPEMTLEKL SVFEANALPV LTVTVRELNT IKALRASVLV RYAEPMGYEP NRQPANRPVA
TLSSSGCGSN TATVGLVAGS DYTVISNGSK SSWNQQDVYH GIRAAWSQST GRGSKVLIID
TGSSDTQENL GSAFNQGLST GRTVERLVTL PRNTIFGIPY GDYETPNDGC GHGTSMAGAC
AAPRGTDGAS VGIAYNASLI TVRAAEDVFL DASREVQGVT DAYLLAGNRA DVRVISMSMG
RLTSSSQMTD AIRYAYGKGK LILCAAGTSF DWSAGVVGVI YPASLPEAVA VTGVKDNLTT
RCDECHVGSD VEFTVVMQRS SNDRRPLTLA MSGDAPSTVG GSSVATASMA GMAAVVWSRY
PTETRAQIMS RLIAASSNRT ARSSSFGWGR VNLATAVGVP LN
//
