ID A0A0H3KRK3_BURM1 Unreviewed; 515 AA.
AC A0A0H3KRK3;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Carboxy-terminal protease {ECO:0000313|EMBL:BAG44698.1};
DE EC=3.4.21.102 {ECO:0000313|EMBL:BAG44698.1};
GN OrderedLocusNames=BMULJ_02810 {ECO:0000313|EMBL:BAG44698.1};
OS Burkholderia multivorans (strain ATCC 17616 / 249).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=395019 {ECO:0000313|EMBL:BAG44698.1, ECO:0000313|Proteomes:UP000008815};
RN [1] {ECO:0000313|EMBL:BAG44698.1, ECO:0000313|Proteomes:UP000008815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249 {ECO:0000313|Proteomes:UP000008815};
RA Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA Hattori M., Tsuda M.;
RT "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL Submitted (APR-2007) 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; AP009385; BAG44698.1; -; Genomic_DNA.
DR RefSeq; WP_006415073.1; NC_010804.1.
DR AlphaFoldDB; A0A0H3KRK3; -.
DR STRING; 395019.BMULJ_02810; -.
DR KEGG; bmj:BMULJ_02810; -.
DR eggNOG; COG0793; Bacteria.
DR HOGENOM; CLU_017295_1_1_4; -.
DR Proteomes; UP000008815; 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:BAG44698.1};
KW Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:BAG44698.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008815};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..515
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002613936"
FT DOMAIN 89..157
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 366..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 515 AA; 56246 MW; D1245E9BC8CADBD7 CRC64;
MRIKLKNIGL IAAGLATGVF ATLQISASAE QTVTAPLPLD QLRLFAEVFG QIKREYVEPV
DDKKLLTAAI KGMVSSLDPH SSFLDKTDYD ELQEQTKGRF AGLGIEISQE DGLVKVISPI
EDTPAFRAGI RPGDLITRIN DKPVRGMTLD KAVKQMRGEP GTKVTLTIFR KSDDRTFPVT
VTRAIIKVQS VKMKMLDPGY AYIRITSFQE RTTPDLAAKL QDIARQQPNL KGLILDLRNN
GGGLLQSAVG VAGAFLPPDS VVVSTNGQIP DSKQVYRDTY DNYRLPSFDG DPLKSLPPIF
KTVPMVVLTN AYSASASEIV AGALQDSKRA LIMGKTTFGK GSVQTVRPMT ADTALRLTTA
YYYTPSGRSI QNKGITPDLP VDQYADGDPD DVLVTREVDY SNHLANTQDP NEKKEQEERE
QRRMDQLRIL EEQNDKKTPE QRQKDRDRKP IEFGSADDFM MQQALNKLEG KPVQESKSLL
AESTKTAAGK PAAAAKASGA AAKPAAAPKP ASAPQ
//