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Database: UniProt
Entry: B2AGP6_CUPTR
LinkDB: B2AGP6_CUPTR
Original site: B2AGP6_CUPTR 
ID   B2AGP6_CUPTR            Unreviewed;       535 AA.
AC   B2AGP6;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   SubName: Full=Carboxy-terminal-processing protease, Peptidase S41 family putative autocatalytic processed {ECO:0000313|EMBL:CAP62945.1};
DE            EC=3.4.21.102 {ECO:0000313|EMBL:CAP62945.1};
GN   OrderedLocusNames=RALTA_A0275 {ECO:0000313|EMBL:CAP62945.1};
OS   Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS   107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=977880 {ECO:0000313|EMBL:CAP62945.1, ECO:0000313|Proteomes:UP000001692};
RN   [1] {ECO:0000313|EMBL:CAP62945.1, ECO:0000313|Proteomes:UP000001692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 /
RC   R1 {ECO:0000313|Proteomes:UP000001692};
RX   PubMed=18490699; DOI=10.1101/gr.076448.108;
RA   Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA   Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA   Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA   Masson-Boivin C.;
RT   "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT   comparative genomics of rhizobia.";
RL   Genome Res. 18:1472-1483(2008).
CC   -!- SIMILARITY: Belongs to the peptidase S41A family.
CC       {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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DR   EMBL; CU633749; CAP62945.1; -; Genomic_DNA.
DR   RefSeq; WP_012351612.1; NC_010528.1.
DR   AlphaFoldDB; B2AGP6; -.
DR   MEROPS; S41.004; -.
DR   GeneID; 29762569; -.
DR   KEGG; cti:RALTA_A0275; -.
DR   eggNOG; COG0793; Bacteria.
DR   HOGENOM; CLU_017295_1_1_4; -.
DR   BioCyc; CTAI977880:RALTA_RS01345-MONOMER; -.
DR   Proteomes; UP000001692; Chromosome 1.
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; 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; PF13180; PDZ_2; 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:CAP62945.1};
KW   Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:CAP62945.1};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..535
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002772823"
FT   DOMAIN          88..156
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          401..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..452
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..476
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..524
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   535 AA;  58406 MW;  C2372B488BFCBB38 CRC64;
     MRKTLKNISL VSVGLVAGVL ATLQISATAQ NSSGPLPLDQ LRLMADIFGQ IKREYVEPVD
     DKKLLTEAIK GMVASLDPHS SYLDEKDFKE LQEGTRGRFA GLGIEISQEE GLVKVINPIE
     DTPAFRAGIQ PGDLITRIDD KPVRGLPLEQ AVKRMRGEPG TKVTLTIYRK SEERTFPVSI
     TRAEIRVQSV KAKMLDNNIG WIRLTSFQER TISDLARKLT ELSQKNPNMK GLVLDLRNNG
     GGVLQGAVGV AAAFLPEDAT VVSTNGQVPD AKRVYKATYN NYRLSSLEDD PLKDLPALFK
     KIPMVVLTNA YSASASEIVA GALQDHHRAQ IMGKTTFGKG SVQTVRPLTN DTGIKLTIAY
     YYTPSGKSIQ AKGIRPDIPV DQNPEGDPDD ALITREIDTE RHLHNKQESE EPEMTEREQR
     RVEELRRLEE ENAKKTPEER EKERRKKPVE FGSADDFMLQ QAIAQLNGQP VKRSKSRLET
     NPPADNGKAA KPSGKSGAKG ASVPAAKPAA PAPGKQPPAS APIGEPLGTP TGKAP
//
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