ID B6B2S7_9RHOB Unreviewed; 494 AA.
AC B6B2S7;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Probable periplasmic serine endoprotease DegP-like {ECO:0000256|ARBA:ARBA00013958};
DE EC=3.4.21.107 {ECO:0000256|ARBA:ARBA00013035};
DE AltName: Full=Protease Do {ECO:0000256|ARBA:ARBA00032850};
GN Name=degQ {ECO:0000313|EMBL:EDZ41021.1};
GN ORFNames=RB2083_535 {ECO:0000313|EMBL:EDZ41021.1};
OS Rhodobacteraceae bacterium HTCC2083.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=314270 {ECO:0000313|EMBL:EDZ41021.1, ECO:0000313|Proteomes:UP000005746};
RN [1] {ECO:0000313|Proteomes:UP000005746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2083 {ECO:0000313|Proteomes:UP000005746};
RX PubMed=21036993; DOI=10.1128/JB.01268-10;
RA Kang I., Vergin K.L., Oh H.M., Choi A., Giovannoni S.J., Cho J.C.;
RT "Genome sequence of strain HTCC2083, a novel member of the marine clade
RT Roseobacter.";
RL J. Bacteriol. 193:319-320(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Acts on substrates that are at least partially unfolded. The
CC cleavage site P1 residue is normally between a pair of hydrophobic
CC residues, such as Val-|-Val.; EC=3.4.21.107;
CC Evidence={ECO:0000256|ARBA:ARBA00001772};
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DR EMBL; DS995276; EDZ41021.1; -; Genomic_DNA.
DR AlphaFoldDB; B6B2S7; -.
DR STRING; 314270.RB2083_535; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_0_5; -.
DR Proteomes; UP000005746; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 2.
DR Gene3D; 2.30.42.10; -; 2.
DR Gene3D; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011782; Pept_S1C_Do.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR NCBIfam; TIGR02037; degP_htrA_DO; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:EDZ41021.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005746};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 273..338
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 369..481
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 126
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 156
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 229
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 494 AA; 52127 MW; B38F25EEE43DA5BD CRC64;
MSQAIVLSQD KQDETRKVLP WTLAMGLSVA LLLLQTMSAA ARGAPESFAD LAEKISPAVV
NITTSTTVAR NTAPRGVAPE GSPFEEFFRE FQDRNRGGNG DRPRRSSALG SGFVISEDGF
VVTNNHVIDG ADEILIEFFE GGELPAKVIG TDPNTDIALL KVETDKPLSF VSFGNSDFSR
VGDWVMAMGN PLGQGFSVSA GIVSARNRAL SGSYDDYIQT DAAINRGNSG GPLFNMDGDV
IGVNTAILSP NGGSIGIGFS MASNVVVNVV DQLKEFGETR RGWLGVRIQD VTDDVAEAIG
LENAAGALVT DVPEGPSMEA GIKAGDVIMS FDGKDVSDTR SLVKTVGNTQ VGKAVRVIVF
RDGKTETLKV TLGRREEAEG AVPASQPAAP AAPSKTEVLG LTISEITDEL RDQLDLTDSA
SGLVIQDVVE TSKAYEKGLR AGDLITEAGQ QKLASVEDLT KQIEAAREAG RKSLLLLVRR
AGDPRFVALA LEEG
//
