ID A0A3S0QUX0_9HYPH Unreviewed; 571 AA. AC A0A3S0QUX0; DT 10-APR-2019, integrated into UniProtKB/TrEMBL. DT 10-APR-2019, sequence version 1. DT 02-OCT-2024, entry version 21. 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=EFQ99_16935 {ECO:0000313|EMBL:RUM24463.1}; OS Rhizobium vallis. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=634290 {ECO:0000313|EMBL:RUM24463.1, ECO:0000313|Proteomes:UP000278823}; RN [1] {ECO:0000313|Proteomes:UP000278823} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCBAU 65647 {ECO:0000313|Proteomes:UP000278823}; RA Huo Y.; RT "Rhizobium chutanense sp. nov., isolated from root nodules of Phaseolus RT vulgaris in China."; RL Submitted (NOV-2018) 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}; CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RUM24463.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; RJTH01000005; RUM24463.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3S0QUX0; -. DR OrthoDB; 9758917at2; -. DR Proteomes; UP000278823; Unassembled WGS sequence. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. 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; 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}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}. FT SIGNAL 1..33 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 34..571 FT /note="Probable periplasmic serine endoprotease DegP-like" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5038874268" FT DOMAIN 305..396 FT /note="PDZ" FT /evidence="ECO:0000259|PROSITE:PS50106" FT DOMAIN 477..526 FT /note="PDZ" FT /evidence="ECO:0000259|PROSITE:PS50106" FT REGION 38..77 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 96..135 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 403..472 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 121..135 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 442..458 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 157 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1" FT ACT_SITE 187 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1" FT ACT_SITE 261 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1" SQ SEQUENCE 571 AA; 58666 MW; 9D603095ABC073A4 CRC64; MAPTIRSPFR RTLALLASAA ILAQAGVSGI AHAQTAPEAA APGMATPPAA AQTAPAPAAP QQVPPIQSTV PNNGPASVAD LAEGLLDAVV NISTSQNVKD DEGAGPAPRA PDGSPFQEFF NDFFNKKQGN KGPNHNVSSL GSGFVIDPTG YIVTNNHVIE GADDIEINFA NGSKLKAKLI GTDTKTDLSV LKVEPKTPLK SVKFGDSSTM RIGDWVMAIG NPFGFGGSVT VGIISGRGRN INAGPYDNFI QTDAAINKGN SGGPLFNMKG EVIGINTAII SPSGGSIGIG FSVPSELASG VVEQLRQFGE TRRGWLGVRI QPVTDDIADS LGLDSAKGAL VAGVIKGGPV DDGSIKAGDV ILKFDGKAVI EMRDLPRVVA ESAVGKQVDV VVLRDGKEQT VKVTLGRLED SDQPGGSDDA APDGSQDDGV ITPDPGENND MDQPDTGDQA QPAPTAPDQH QGQGHAAPDA ATPKNVLGLS LSLLSPETRK AFGIAESVDG VVVTEVTPGS ASAEKGLKPG DVIVEVAQEF MKSPDAVAAK VQSLKQEGRR NAQLMIASAN GDLRFVAVPM E //