ID A0A1G7UKJ6_9BRAD Unreviewed; 501 AA.
AC A0A1G7UKJ6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 ORFNames=SAMN05216338_1001441 {ECO:0000313|EMBL:SDG47751.1};
OS Bradyrhizobium sp. Rc2d.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1855321 {ECO:0000313|EMBL:SDG47751.1, ECO:0000313|Proteomes:UP000198770};
RN [1] {ECO:0000313|EMBL:SDG47751.1, ECO:0000313|Proteomes:UP000198770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rc2d {ECO:0000313|EMBL:SDG47751.1,
RC ECO:0000313|Proteomes:UP000198770};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Might be efficient in the degradation of transiently
CC denatured and unfolded proteins which accumulate in the periplasm
CC following stress conditions. {ECO:0000256|ARBA:ARBA00002610}.
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; FNCU01000001; SDG47751.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7UKJ6; -.
DR STRING; 1855321.SAMN05216338_1001441; -.
DR OrthoDB; 7358927at2; -.
DR Proteomes; UP000198770; 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:SF130; PERIPLASMIC SERINE ENDOPROTEASE DEGP-LIKE; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR Pfam; PF13180; PDZ_2; 2.
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:SDG47751.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..36
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 37..501
FT /note="Probable periplasmic serine endoprotease DegP-like"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039321279"
FT DOMAIN 278..369
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 390..489
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 92..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 130
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 160
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 234
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 501 AA; 52444 MW; DC6A6683BDA0A689 CRC64;
MIAATIAPSR LRHWVRTGLA ALAIGAFGAF GTPAHARGPD GIADVAEKVI DAVVNISTSQ
TVDAKGGGSN TMPQLPPGSP FEEFFDDFFK NRRGPGGGSK GGDNNPPRKT NSLGSGFIID
TSGVVVTNNH VIADADEIHV ILNDGTKIKA ELVGVDKKTD LAVLKIKPPK PLVAVKFGDS
DKLRLGDWVV AIGNPFSLGG TVTAGIVSAK NRDISSGPYD SYIQTDASIN RGNSGGPLFN
LDGDVIGVNT LIISPSGGSI GIGFAVPSKT VVGVVDQLRQ FGELRRGWLG VRIQSVTDEI
AESLSIKPAR GALIAGVDDK GPAKPAGIEP GDVVVKFDGK DVKDPKDLSR VVADTAVGKE
VDVIIIRKGQ EQTKKVTLGR LQDPEKVQAA VKTDEPAPEK PVTQKALGLD LATLSKDLRT
RYKIKDTVKG VVVTSVDANS DAAEKRLSAG DVIVEVAQEA VSSGAEIQKR VDQLKKDGKK
SVLLLVSNAD GELRFVALSV Q
//
