ID   A0A136LNQ5_9CHLR        Unreviewed;       606 AA.
AC   A0A136LNQ5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Peptidase S8/S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:KXK23294.1};
DE   Flags: Fragment;
GN   ORFNames=UZ15_CFX003000670 {ECO:0000313|EMBL:KXK23294.1};
OS   Chloroflexi bacterium OLB15.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1617416 {ECO:0000313|EMBL:KXK23294.1, ECO:0000313|Proteomes:UP000070332};
RN   [1] {ECO:0000313|EMBL:KXK23294.1, ECO:0000313|Proteomes:UP000070332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB15 {ECO:0000313|EMBL:KXK23294.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
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       ECO:0000256|RuleBase:RU003355}.
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:KXK23294.1}.
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DR   EMBL; LMZS01000035; KXK23294.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136LNQ5; -.
DR   STRING; 1617416.UZ15_CFX003000670; -.
DR   Proteomes; UP000070332; 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; 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; 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          244..453
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   REGION          47..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          470..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        473..487
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        252
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        285
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        438
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   NON_TER         606
FT                   /evidence="ECO:0000313|EMBL:KXK23294.1"
SQ   SEQUENCE   606 AA;  61950 MW;  BBA536F68E36B602 CRC64;
     MARKHILGLF VLGLFLLAIF AVIAVAIRPA PQEVVAMPTL MSLPTVTETN TPTDIPTLPP
     NTDTPTEAPA APTSTIEEAA PISAETSRPT ESLAPTVPTN TATATATSVP TEIPPTAEIA
     PTVPPVVIIN SSAPEVVQPP APAVENVVVI AFESDSSAEE RAAYIESING EVESSIEALN
     TVVVSVPDTV TAQALSAAPI VAQTEPDYFA TVLTAPDDPL YSQQWALQAI GAESAWGELP
     ADAQQITVAV IDTGICADHA ELQGRILAGY DFVDDDAVPQ DEYGHGCAVA GIIAAQANNA
     QGIAGLAPNA QILPLRVLNG AGYGSYSDIA EAIIYAVDQG AQVINLSLGG VNPSSLLEDA
     VSYAMAHGRQ VVAAAGNNFG GAVMYPAAYA PVISVGSVDQ NLQHSSFNPA GVLDVYAPGR
     DISSLAINGA YTSLTGTSLA APHVSAAIAI SMALGEPFVA TGQVLSLGEG GLTPTLPPTS
     TPEATPEGET LPETEPIIFD RDAAERPTYP VTSDLYQLAQ AYEQSAAQAQ AFADTTLLQV
     NGEQVLVEIT VSDEGAIPSV VNALGSIGAQ VTASGSGVIV AYIPFGQIEA AATLPGVRYI
     QSALPP
//