ID A0A1W1UXT8_DESTI Unreviewed; 388 AA.
AC A0A1W1UXT8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Carboxyl-terminal processing protease {ECO:0000313|EMBL:SMB85571.1};
GN ORFNames=SAMN00017405_1652 {ECO:0000313|EMBL:SMB85571.1};
OS Desulfonispora thiosulfatigenes DSM 11270.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulfonispora.
OX NCBI_TaxID=656914 {ECO:0000313|EMBL:SMB85571.1, ECO:0000313|Proteomes:UP000192731};
RN [1] {ECO:0000313|EMBL:SMB85571.1, ECO:0000313|Proteomes:UP000192731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11270 {ECO:0000313|EMBL:SMB85571.1,
RC ECO:0000313|Proteomes:UP000192731};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FWWT01000012; SMB85571.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1UXT8; -.
DR STRING; 656914.SAMN00017405_1652; -.
DR Proteomes; UP000192731; Unassembled WGS sequence.
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 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; 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 SMART; SM00228; PDZ; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50156; PDZ domain-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, ECO:0000313|EMBL:SMB85571.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000192731};
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..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 100..156
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 388 AA; 42192 MW; 1C799CEA7547F95C CRC64;
MLHLQTTKKI LKVVLTIFTI ISFIVTSVVG YIFITNYNQV GQLLHVATLV KSSYLHPITT
EQLVEGATKG LVDSLGDEYS VFLDEKEFQK LQSYIEPTFG GIGVYVGTKE KDITVIAPVE
GTPGHKAGIK SGDIITKIDG KSTTGMTLDD AVEVMRGEPG TKVKLSIKRE GTDKILDFSI
IREIVDVPTV KAEILKENKD IAYLAITLFG NNTDEEFTAE MEKINKEGYK GLIIDLRNNP
GGNLETVVSI LKEVLPESPI VHIVDKNGKS VTYSSKGPGI KVPLVVLVNE GSASASEIFA
GAVKDTKLGT LVGEKTYGKG VVQNVFFLKD GAGLKLTTAK YLTPNKNDIH KLGIKPDEEV
KLPLITGSEE FIEDTQLKKA IELLQGKL
//
