ID R7RSS1_9CLOT Unreviewed; 397 AA.
AC R7RSS1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Carboxyl-terminal protease {ECO:0000313|EMBL:CDF58305.1};
DE EC=3.4.21.102 {ECO:0000313|EMBL:CDF58305.1};
GN ORFNames=TCEL_00351 {ECO:0000313|EMBL:CDF58305.1};
OS Thermobrachium celere DSM 8682.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Thermobrachium.
OX NCBI_TaxID=941824 {ECO:0000313|EMBL:CDF58305.1, ECO:0000313|Proteomes:UP000014923};
RN [1] {ECO:0000313|EMBL:CDF58305.1, ECO:0000313|Proteomes:UP000014923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8682 {ECO:0000313|EMBL:CDF58305.1,
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, ECO:0000256|RuleBase:RU004404}.
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:CDF58305.1}.
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DR EMBL; CAVN010000097; CDF58305.1; -; Genomic_DNA.
DR RefSeq; WP_018662260.1; NZ_HF952018.1.
DR AlphaFoldDB; R7RSS1; -.
DR eggNOG; COG0793; Bacteria.
DR HOGENOM; CLU_017295_3_2_9; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000014923; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:CDF58305.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:CDF58305.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014923};
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..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 102..167
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 397 AA; 43981 MW; 3C3191E39726B89C CRC64;
MDKRQVSVKR VIALIIITNL ITASLLIFAP IPFIGGKKLV SNEEYQFVKK FNKLISIKTI
LEKKYVDKID EDKLVEGAVR GMVDGIGDPY TVFLNQKEFE ELLTHTRGSY AGVGLYVGEK
DGKIIVVAPI EDTPAYRAGI QSGDYILKVN DQDVSAKEMD KAVSMMKGKE GTKVKLTIYR
EGKGTLEFEL TRAIITIKTV KSDVIENDIG YIRITTFDEH TADAFNKALD NLLSKGIKGL
IIDLRDNPGG LLDQCTQIAD RILGEGTIVY TIDNQGKREE WKSDSNKLNI PLVLLVNEGS
ASASEILSGA VRDFKAGTLI GTKTFGKGLV QEIISLPNKE GLKVTIARYY TPSGECIQGK
GIEPHIKLDL PQKDKIKELS YKEDIQIQKA IEVLRNK
//
