ID R7RM63_9CLOT Unreviewed; 518 AA.
AC R7RM63;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Carboxyl-terminal processing protease {ECO:0000313|EMBL:CDF57257.1};
GN ORFNames=TCEL_01171 {ECO:0000313|EMBL:CDF57257.1};
OS Thermobrachium celere DSM 8682.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Thermobrachium.
OX NCBI_TaxID=941824 {ECO:0000313|EMBL:CDF57257.1, ECO:0000313|Proteomes:UP000014923};
RN [1] {ECO:0000313|EMBL:CDF57257.1, ECO:0000313|Proteomes:UP000014923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8682 {ECO:0000313|EMBL:CDF57257.1,
RC ECO:0000313|Proteomes:UP000014923};
RA Ciranna A., Larjo A., Kivisto A., Santala V., Roos C., Karp M.;
RT "Draft genome sequence of the hydrogen-ethanol-producing anaerobic
RT alkalithermophilic Caloramator celere.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179}.
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:CDF57257.1}.
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DR EMBL; CAVN010000086; CDF57257.1; -; Genomic_DNA.
DR AlphaFoldDB; R7RM63; -.
DR eggNOG; COG0793; Bacteria.
DR HOGENOM; CLU_017295_3_1_9; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000014923; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
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; 2.30.30.40; SH3 Domains; 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; IPR003646; SH3-like_bac-type.
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; PF08239; SH3_3; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00287; SH3b; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS51781; SH3B; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW Protease {ECO:0000313|EMBL:CDF57257.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014923};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 91..145
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 456..518
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
SQ SEQUENCE 518 AA; 58787 MW; 04BDFB6FBC84BA69 CRC64;
MPMRLNLKQK IVSFLIVIMV LFQLNVFAEA QLEEVKEIIK NYYVENVDDS KLNVNSVEEL
INNLNDPYTA YFTKDEFDSF IGSINQSYVG VGIVVEKCEE GILITSVLDN SSAKQAGILP
GDVIVEINGL SIVDRSLEDA ISLIRGEEGT YVNLKVKRDN QILSFNLKRL KIELATVKGS
LIDGHVGYIN LMSFGENTNS EFLSVYNNLK SKGADFFILD VRNNGGGFLY TAVEILSNFI
GSNTCVVLKD KYGFQTKVKN DVVPSRLINE RFILLTNGNS ASASEILAAA LKDYNKALII
GNRTFGKGTA QSFFVLSNGD ILKLTTQKFY SPNGNEINKI GVLPHIRIYE DIDKVALMLT
EREPVADKTN YVKLVINGKM YYINLKNDTY FNKLISSINN CEMYIGVKNY WVKRDLNYYK
QKENAFVEVK RDINNKIKEI EKYHTVDAAK KSNFNTKYGY VAVSKLNFRQ IPKLKGKVLF
VLNKGTKFEI LESSMGWYKI KYNNRIAYVY GKYIKLTK
//
