ID   A0A0N8PSB3_9CHLR        Unreviewed;       493 AA.
AC   A0A0N8PSB3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Peptidase C-terminal archaeal/bacterial domain-containing protein {ECO:0000259|Pfam:PF04151};
GN   ORFNames=SE17_16635 {ECO:0000313|EMBL:KPV52245.1};
OS   Kouleothrix aurantiaca.
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC   Roseiflexaceae; Kouleothrix.
OX   NCBI_TaxID=186479 {ECO:0000313|EMBL:KPV52245.1, ECO:0000313|Proteomes:UP000050509};
RN   [1] {ECO:0000313|EMBL:KPV52245.1, ECO:0000313|Proteomes:UP000050509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COM-B {ECO:0000313|EMBL:KPV52245.1,
RC   ECO:0000313|Proteomes:UP000050509};
RA   Hemp J.;
RT   "Draft genome sequence of Kouleothrix aurantiaca JCM 19913.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:KPV52245.1}.
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DR   EMBL; LJCR01000609; KPV52245.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N8PSB3; -.
DR   Proteomes; UP000050509; Unassembled WGS sequence.
DR   Gene3D; 2.60.120.380; -; 1.
DR   InterPro; IPR007280; Peptidase_C_arc/bac.
DR   PANTHER; PTHR48184; RICIN B-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR48184:SF1; RICIN B-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF04151; PPC; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000050509};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..493
FT                   /note="Peptidase C-terminal archaeal/bacterial domain-
FT                   containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006029317"
FT   DOMAIN          401..474
FT                   /note="Peptidase C-terminal archaeal/bacterial"
FT                   /evidence="ECO:0000259|Pfam:PF04151"
FT   REGION          24..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          241..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..291
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..306
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..332
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   493 AA;  52212 MW;  CCB6735FFB46D9C0 CRC64;
     MTRKHLAMLL AVVVVGMMVQ QPSTAQVRST PPHDASVNGG QAGSLSARPA SSAQSAQEQV
     GIANVLMNEG FEGTWPNAGW TVFDNSASGR DYLWGRRACQ PQLGSYSGMA AGGGTLGSSR
     ACGSAYPNGL NSWAIYGPID LSAASSASVS YAFRGRSEGA SDANGRPFDA LVVGSNTQLY
     GNYSGWLWWG NWSGSYNQKT LDLSDRLGQP QVWIGFAFYS DASVNDIGFT IDSLRIDVTY
     APPSNTPTPT DTPTNTPTDT PTDTATPTDT ATPTDTPTNT PTATDTPAPT DTPEISPTPS
     ETPQFSPTPT DTPTNTPTDT ATPTDTPTPS NTPTISPVGP PEPQPPLYIP VALFYPTGCV
     APLVLVGDTD TPLEAPRLHG PSLRCSGREQ ITSGADTAED QWYAIDLKAQ QQLTFDLTNV
     PDGADYDVYL FDSKVVGPEA ATAKFLTQSI APRNSSESIA FTSKAAATYY LRIYMVHKAI
     RAPNTYVLKL EVK
//