ID   A0A1H1DHH9_9GAMM        Unreviewed;       506 AA.
AC   A0A1H1DHH9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Serine protease {ECO:0000313|EMBL:SDQ75922.1};
GN   ORFNames=SAMN05216569_1940 {ECO:0000313|EMBL:SDQ75922.1};
OS   Pseudoxanthomonas sp. CF125.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=1855303 {ECO:0000313|EMBL:SDQ75922.1, ECO:0000313|Proteomes:UP000199049};
RN   [1] {ECO:0000313|EMBL:SDQ75922.1, ECO:0000313|Proteomes:UP000199049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF125 {ECO:0000313|EMBL:SDQ75922.1,
RC   ECO:0000313|Proteomes:UP000199049};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FNLD01000002; SDQ75922.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1DHH9; -.
DR   STRING; 1855303.SAMN05216569_1940; -.
DR   Proteomes; UP000199049; 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   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; 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   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; 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:UP000199049};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          169..468
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        178
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        244
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        429
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   506 AA;  52617 MW;  41AAF188C89D3F0C CRC64;
     MKIRWILGSR WSGTVALACL GLCMTGTVLA REKAQTERLA HQESYDQFIV RYKEGTATAS
     SDNLLRSSID RAAARLSNAL GKSVSASKVR RMSGSSDVIR TSRLLDRVEA AMLMRQFAED
     PDVVHVEPDL TISALADTND PYFTAQWHLQ GGVAANGTNA KFAWDTAIGT GIVIAIIDSG
     FTAHPDLDPA RIVPGYDFIT NTVIAKDGNG RDSDASDPGS YSQGIILECP SELFCNTLGD
     STWHGTRVAG VAAATGNNGY GGAGVAYGAK LMSVRVLGKG GRGKLSDLVD AIKWAGGVAA
     AGLPPLPAVA NRPKVINLSL GFSTATACSV ELQNAINLAY AQGVTVVAAA GNSSSLSDSE
     PAKCENVISV AATNNLGDRS DFSSYADWIT IAAPGGQGYD GDADDILTTS NSGWDGPIAP
     NFYEAAGTSM SAPQVSGAVA ILLSHAAARG NCGLSPLQIR SLLMNGARPF PVAQPADKKI
     GAGILDISHS LFEISRVCDV MIPPNP
//