ID A0A1B3LPM1_9PROT Unreviewed; 462 AA.
AC A0A1B3LPM1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=PDZ domain-containing protein {ECO:0000259|PROSITE:PS50106};
GN ORFNames=BSY238_1483 {ECO:0000313|EMBL:AOF82800.1};
OS Methyloversatilis sp. RAC08.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sterolibacteriaceae; Methyloversatilis.
OX NCBI_TaxID=1842540 {ECO:0000313|EMBL:AOF82800.1, ECO:0000313|Proteomes:UP000094168};
RN [1] {ECO:0000313|Proteomes:UP000094168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RAC08 {ECO:0000313|Proteomes:UP000094168};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) 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; CP016448; AOF82800.1; -; Genomic_DNA.
DR RefSeq; WP_069038546.1; NZ_CP016448.1.
DR AlphaFoldDB; A0A1B3LPM1; -.
DR STRING; 1842540.BSY238_1483; -.
DR KEGG; metr:BSY238_1483; -.
DR PATRIC; fig|1842540.3.peg.1492; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000094168; Chromosome.
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; 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};
KW Protease {ECO:0000256|RuleBase:RU004404};
KW Reference proteome {ECO:0000313|Proteomes:UP000094168};
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..462
FT /note="PDZ domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008549321"
FT DOMAIN 89..157
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 406..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 462 AA; 49661 MW; 05245ECCC34690A6 CRC64;
MQKKLQQTGL IMIGLCAGVL LSLNFSANAN KTPGSSLPVE ELRQFADVLN AVKASYVEPV
DDKKLITQAI SGMLSGLDPH SAYLDQDAFK DLQAGTQGEF GGLGIEVGME DGFVKVVSPI
EDTPAFRAGI KSGDLIIKLD DTSTKGLNLS DAVKRMRGKP NTSIRLTIAR KGETKPIEVT
LMREVIKVQS VKSKLVEPGY GYLRLTQFQE QSAEDLAKHI GKLYKDGELK GLVLDLRNDP
GGLLHGAVGV SAAFLQPKAL VVSTDGRTDD AKRRFIASPE DYLRGSRDDF LQTLPAGAKS
VPLVVLVNSG SASASEIVAG ALQDHKRAVI MGTQTFGKGS VQTIMPLTNN TAIKLTTARY
YTPNGRSIQA KGIVPDIVVE ESANGSSGMR LREADLDRHL NNDKDVEIPA MPADPGAKGK
PAPAKEDEDD KQAAPFEFAT KTDYQFTQAL NLLKGLQIMQ KN
//