ID   A0A257B7V3_9BACT        Unreviewed;       434 AA.
AC   A0A257B7V3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Serine protease {ECO:0000313|EMBL:OYT72934.1};
GN   ORFNames=CFK52_03590 {ECO:0000313|EMBL:OYT72934.1};
OS   Chloracidobacterium sp. CP2_5A.
OC   Bacteria; Acidobacteriota; Blastocatellia; Chloracidobacterium.
OX   NCBI_TaxID=2012633 {ECO:0000313|EMBL:OYT72934.1, ECO:0000313|Proteomes:UP000216393};
RN   [1] {ECO:0000313|EMBL:OYT72934.1, ECO:0000313|Proteomes:UP000216393}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CP2_5A {ECO:0000313|EMBL:OYT72934.1};
RA   Ward L.M., Mcglynn S.E., Fischer W.;
RT   "Draft genome of Chloracdibacterium sp. CP2_5A, a phototrophic
RT   Acidobacteria from a Japanese hot spring.";
RL   Submitted (JUN-2017) 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:OYT72934.1}.
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; NKPT01000006; OYT72934.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257B7V3; -.
DR   Proteomes; UP000216393; 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; 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.
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          69..405
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        78
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        119
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        358
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   434 AA;  47464 MW;  39C281B5337BC3DE CRC64;
     MSRLSRDLLH FNLPHWDERE GVCRDCLERF THARARVGLY LSPTSSPSLS RFKILPTPLR
     LGASPRYTGR GVTIAFLDSG FYPHPDITQP VNRILHYHNV LTRRTDPAEL SAPDDSSWHG
     LMTSVVAAGN GFLSKGLYRG IASSARLALV KVGTTRRIYH DDIRRGLDWV YRNRERFGIR
     IVNISCGGDY EASYLTDALS QSAERLVRAG VVVVAASGNA GHQAEHPVLP PASAPSVIAV
     GGFDDKNTLD PNEHDVYQSS YGVTPDGLQK PEVIAPSIWI AAPILPGTPT AQQAALYEEL
     TRAHDGDLKA LLAQHAGIDA ELDAAAHLEP YQLRLLVEGK MRNEKVISGH YKHVDGTSFA
     APIVSSIVAQ MLEVNPRLTP QQVKRILIRT ARRLPNIEPD RQGWGVVNAR QAVAAALNGG
     DALLSGNHLD LNRL
//