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Database: UniProt
Entry: A0A160SXP0_9CHLR
LinkDB: A0A160SXP0_9CHLR
Original site: A0A160SXP0_9CHLR 
ID   A0A160SXP0_9CHLR        Unreviewed;       373 AA.
AC   A0A160SXP0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN   ORFNames=CFX0092_A0035 {ECO:0000313|EMBL:CUS01916.1};
OS   Candidatus Promineifilum breve.
OC   Bacteria; Chloroflexota; Ardenticatenia; Candidatus Promineifilales;
OC   Candidatus Promineifilaceae; Candidatus Promineifilum.
OX   NCBI_TaxID=1806508 {ECO:0000313|EMBL:CUS01916.1, ECO:0000313|Proteomes:UP000215027};
RN   [1] {ECO:0000313|EMBL:CUS01916.1, ECO:0000313|Proteomes:UP000215027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cfx-K {ECO:0000313|EMBL:CUS01916.1,
RC   ECO:0000313|Proteomes:UP000215027};
RA   Oliw E.H.;
RL   Submitted (JAN-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}.
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DR   EMBL; LN890655; CUS01916.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A160SXP0; -.
DR   KEGG; pbf:CFX0092_A0035; -.
DR   OrthoDB; 9798386at2; -.
DR   Proteomes; UP000215027; Chromosome i.
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:UP000215027};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          47..309
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        56
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        93
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        287
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   373 AA;  39110 MW;  751E0E5A822BECCC CRC64;
     MSNAQMPSEI DPVERPRQFD RPLFPHLPEV DSFLWVSQAR AAFNVSGAGQ TVAVLDTGLN
     TGHVDFAGRV VAQANFTPDN GGNPNDAGDG NGHGTNVGGI IVANGDHKGI APGANIVPIK
     VLGNTGGGSF AWIRDALTWV RDNGPAHGVS AVCMSLGDSG NYISDTDYAA DAVRGLIVEL
     RAQRVAVVIA AGNGFFQHNS AQGMSYPAIL RECISVGAVY DAAEGGFAYG SGATAHSSRP
     GQITPFSQRL HKSINRLTQT DIFAPGAPVT SSGINGPNGE SVQHGTSQAT PVTVGVILLM
     QEFHRRLTGE LPEVGDLLAW LIRGGVPIID GDDEDDNVQH TNLSFVRLDA LSALDATRRA
     IQKRLLLEAQ PIG
//
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