ID A0A3S0QUX0_9HYPH Unreviewed; 571 AA. AC A0A3S0QUX0; DT 10-APR-2019, integrated into UniProtKB/TrEMBL. DT 10-APR-2019, sequence version 1. DT 22-FEB-2023, entry version 15. DE RecName: Full=Periplasmic serine endoprotease DegP-like {ECO:0000256|RuleBase:RU364067}; DE EC=3.4.21.107 {ECO:0000256|RuleBase:RU364067}; GN ORFNames=EFQ99_16935 {ECO:0000313|EMBL:RUM24463.1}; OS Rhizobium vallis. OC Bacteria; Proteobacteria; 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 -!- 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 ECO:0000256|RuleBase:RU364067}; CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|RuleBase:RU364067}. CC -!- SIMILARITY: Belongs to the peptidase S1C family. CC {ECO:0000256|RuleBase:RU364067}. 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:0004222; F:metalloendopeptidase activity; IEA:InterPro. 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; IPR041489; PDZ_6. DR InterPro; IPR036034; PDZ_sf. DR InterPro; IPR011782; Pept_S1C_Do. DR InterPro; IPR008915; Peptidase_M50. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR001940; Peptidase_S1C. DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1. DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1. DR Pfam; PF13180; PDZ_2; 1. DR Pfam; PF17820; PDZ_6; 1. DR Pfam; PF02163; Peptidase_M50; 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 TIGRFAMs; TIGR02037; degP_htrA_DO; 1. DR PROSITE; PS50106; PDZ; 2. PE 3: Inferred from homology; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364067}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364067}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Serine protease {ECO:0000256|RuleBase:RU364067}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364067}; KW Stress response {ECO:0000256|RuleBase:RU364067}. FT SIGNAL 1..33 FT /evidence="ECO:0000256|RuleBase:RU364067" FT CHAIN 34..571 FT /note="Periplasmic serine endoprotease DegP-like" FT /evidence="ECO:0000256|RuleBase:RU364067" FT /id="PRO_5018381433" 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 //