ID L0EAX6_THECK Unreviewed; 476 AA.
AC L0EAX6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=C-terminal processing peptidase {ECO:0000313|EMBL:AGA56831.1};
GN OrderedLocusNames=Theco_0621 {ECO:0000313|EMBL:AGA56831.1};
OS Thermobacillus composti (strain DSM 18247 / JCM 13945 / KWC4).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Thermobacillus.
OX NCBI_TaxID=717605 {ECO:0000313|EMBL:AGA56831.1, ECO:0000313|Proteomes:UP000010795};
RN [1] {ECO:0000313|Proteomes:UP000010795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18247 / JCM 13945 / KWC4
RC {ECO:0000313|Proteomes:UP000010795};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Anderson I.,
RA Woyke T.;
RT "Complete sequence of chromosome of Thermobacillus composti KWC4.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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DR EMBL; CP003255; AGA56831.1; -; Genomic_DNA.
DR AlphaFoldDB; L0EAX6; -.
DR STRING; 717605.Theco_0621; -.
DR KEGG; tco:Theco_0621; -.
DR eggNOG; COG0793; Bacteria.
DR eggNOG; COG3409; Bacteria.
DR HOGENOM; CLU_017295_3_0_9; -.
DR Proteomes; UP000010795; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00988; PDZ_CTP_protease; 1.
DR CDD; cd07560; Peptidase_S41_CPP; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.750.44; -; 1.
DR Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR InterPro; IPR005151; Tail-specific_protease.
DR NCBIfam; TIGR00225; prc; 1.
DR PANTHER; PTHR32060:SF22; CARBOXYL-TERMINAL-PROCESSING PEPTIDASE 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004404};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU004404};
KW Reference proteome {ECO:0000313|Proteomes:UP000010795};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 97..178
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 476 AA; 52247 MW; 13C444AFBAA53820 CRC64;
METDSKMKRR GAGLLVVLAV LLVTVAAGFL AGRWWMMERY PMLKDPAFAN LDYTYREIMS
DYLYGADSSE LIHGAAKGMA ASLRDPYSAY YAGEEGKEYV QRYDDHIVGI GVEIREEDGE
FVVTSAYKGA PADEAGIRKD DVIVAVDGVS MKGKSMQELV SRTRGEVGTK VTITIRRDGL
TEPFDVTLVR EEIPVTTVYA EMLEDGIGKV QITRFAEGTG KEFGKAVDEL LAQGMRGLLL
DLRSNPGGLL SSTLEVASRL IPKDKVILEV VYKDEKRRIT YTSTQSKAWD KPITVLIDES
SASSAEVLAA ALRDSAGAKL VGMKTFGKGV VQMFRPLKDG SVLKLTESEW VTPSGGRINN
VGIEPHVAVE LPDYASLPAL PTDEVLKVGS LGQDVRTAER MLEAVGYDPG EPEGIYDERT
AAAVERFQRD ERLTPTGTIS GRTAFKLMDR LRTKLKEEDP QLKEAVRTLR GMIEGK
//
