ID Q89S21_BRADU Unreviewed; 528 AA.
AC Q89S21;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 126.
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=dop {ECO:0000313|EMBL:BAC47856.1};
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=224911 {ECO:0000313|EMBL:BAC47856.1, ECO:0000313|Proteomes:UP000002526};
RN [1] {ECO:0000313|Proteomes:UP000002526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110
RC {ECO:0000313|Proteomes:UP000002526};
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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; BA000040; BAC47856.1; -; Genomic_DNA.
DR RefSeq; NP_769231.1; NC_004463.1.
DR AlphaFoldDB; Q89S21; -.
DR STRING; 224911.AAV28_09920; -.
DR EnsemblBacteria; BAC47856; BAC47856; BAC47856.
DR KEGG; bja:blr2591; -.
DR PATRIC; fig|224911.5.peg.2558; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_0_5; -.
DR InParanoid; Q89S21; -.
DR OrthoDB; 7358927at2; -.
DR PhylomeDB; Q89S21; -.
DR Proteomes; UP000002526; Chromosome.
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:SF101; PERIPLASMIC PH-DEPENDENT SERINE ENDOPROTEASE DEGQ; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 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:BAC47856.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002526};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 309..380
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 436..492
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 421..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 167
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 197
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 270
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 528 AA; 54655 MW; 2D2812FACDA52BA9 CRC64;
MLRARRHLTQ HGHFDMNDRV NSDITTSRRI LKPRRLALLG TVAALGVAVL AASPGSSPLG
VTSFIAPAQA AESAATPPGF GDLVARVKPA VISVRVRIDQ DNDKSAMLQQ NRMDSDEDAP
FDQFSRQFGF RLPGGMNGMP RQRHQMVTGE GSGFFISADG YAVTNNHVVD HAESVQVTMD
DGTSYTAKVV GTDPKTDLAL IKVDGKKDFP FVKFSDQKPR IGDWVVAVGN PFGLGGTVTA
GIVSASGRDI GNGPYDDFIQ IDAPINKGNS GGPAFDMSGN VIGVNTAIFS PSGGSVGIGF
DIPATTAKLV VAQLKDKGAV TRGWLGVQVQ PVTSEIADSL GLKEARGAIV DNPQDNSPAA
KAGIEAGDVI TAVNGTAIKD SRDLARTVAT LAPGTSVKLD VFHKGASKTV TLALGELPNE
RQAQGKADEG KAQPGNGTPR LGLSLAPAGD VQGAGQKGVV VTEVDPQGPA AQRGIQTGDV
ILNVGGKPVA NVGDVRAELA QAKSSGKNSV LLQIRSADAT RFVAVPLA
//
