ID A0A179D535_9BACT Unreviewed; 424 AA.
AC A0A179D535;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Carboxyl-terminal protease {ECO:0000313|EMBL:OAQ21156.1};
GN ORFNames=TDIS_0808 {ECO:0000313|EMBL:OAQ21156.1};
OS Thermosulfurimonas dismutans.
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfobacteriaceae; Thermosulfurimonas.
OX NCBI_TaxID=999894 {ECO:0000313|EMBL:OAQ21156.1, ECO:0000313|Proteomes:UP000078390};
RN [1] {ECO:0000313|EMBL:OAQ21156.1, ECO:0000313|Proteomes:UP000078390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S95 {ECO:0000313|EMBL:OAQ21156.1,
RC ECO:0000313|Proteomes:UP000078390};
RA Mardanov A.V., Beletsky A.V., Kadnikov V.V., Slobodkin A.I., Ravin N.V.;
RT "Genome analysis of Thermosulfurimonas dismutans, the first thermophilic
RT sulfur-disproportionating bacterium of the phylum Thermodesulfobacteria.";
RL Submitted (APR-2016) 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:OAQ21156.1}.
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DR EMBL; LWLG01000003; OAQ21156.1; -; Genomic_DNA.
DR RefSeq; WP_068669553.1; NZ_LWLG01000003.1.
DR AlphaFoldDB; A0A179D535; -.
DR STRING; 999894.TDIS_0808; -.
DR PATRIC; fig|999894.6.peg.805; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000078390; Unassembled WGS sequence.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|RuleBase:RU004404};
KW Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:OAQ21156.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}.
FT DOMAIN 83..151
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 375..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 200..227
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 424 AA; 47280 MW; 1DC9D1A626194674 CRC64;
MKRKVSVIIL LLWTFFGCSC IYAKEANRKE DPYEALKLFS QVLELVEENY VKEVATKDLI
YGAIEGMLAN LDPHSSFLKP EDYKELQIET KGSFTGIGIE ITIKDGVLTV VAPIEGTPAW
KAGLKSGDKI IKINGKPTKG ISLMEAVKLL RGPKGTKVTI SIFREGFKEL KDITIVRDVI
PIKSVRFQTL EPGYGYVRIS SFQEKTAKEL REALQKLEKQ NKPLKGLVLD LRNNPGGLLE
AAVEVADEFL DEGLIVYTKG RRKDQNFEFK ARPNRHKHAY PIVILVNAGT ASASEIVAGA
LQDHHRAVIL GTKTFGKGSV QTIIPLPDGS AVRLTTAQYY TPSGRSIQAE GIEPDLEIPE
IKPDCLRNHP LIREKDLEGH LENPEKTSDN ETTTKAQDLL KKDFQLREAL KVLKSLKAFS
QIKY
//
