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Database: UniProt
Entry: A0A0W1DX70_9SPHN
LinkDB: A0A0W1DX70_9SPHN
Original site: A0A0W1DX70_9SPHN 
ID   A0A0W1DX70_9SPHN        Unreviewed;       425 AA.
AC   A0A0W1DX70;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Serine protease {ECO:0000313|EMBL:KTE22690.1};
GN   ORFNames=ATE67_01800 {ECO:0000313|EMBL:KTE22690.1};
OS   Sphingopyxis sp. H050.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1759072 {ECO:0000313|EMBL:KTE22690.1, ECO:0000313|Proteomes:UP000053439};
RN   [1] {ECO:0000313|Proteomes:UP000053439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H050 {ECO:0000313|Proteomes:UP000053439};
RA   Gomez-Alvarez V., Revetta R.P.;
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KTE22690.1}.
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DR   EMBL; LNRZ01000001; KTE22690.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W1DX70; -.
DR   STRING; 1759072.ATE67_01800; -.
DR   OrthoDB; 5405281at2; -.
DR   Proteomes; UP000053439; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05561; Peptidases_S8_4; 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; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 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};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          183..416
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        189
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        217
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        368
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   425 AA;  42810 MW;  FDBE781D96C2CC65 CRC64;
     MMRVTAILLL IASLLLISVG IGQKVSAQVA LPPVQLPDAA RTIPPLPSVG ADPLITVADT
     LADVRLNRIA ALVRGHRDSI ELDERGEPAV RGVLVATGID DAMVASAAKQ GFALIDREHV
     EGLDLDIARF RVPEGRSLAR ARKQLAKLLP AAEVDVDNIY FASGPGGALS GAALAAPSAG
     GAASLGLIDG GVAAHPSLGG RVEQRGFARG APAASKHGTA VASLLIGNGA VRGSAPGQRL
     RAADVYGSDP AGGNASAIAR ALGWLAQGGV AVTTISLVGP DNKLLAAAIQ RAQQRGMLVV
     AAVGNDGPAA PPAYPASYRG VFAVTGVDAK DRVLPEAGRA LHVDFAAPGD AVLAATGAAS
     SERLRGTSFA APLVAGRLAL RYPAPGIDRI GPAVAAMVME ARDLGKKGRD KLYGHGLICG
     TCGGR
//
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