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Database: UniProt
Entry: Q2K6H2_RHIEC
LinkDB: Q2K6H2_RHIEC
Original site: Q2K6H2_RHIEC 
ID   Q2K6H2_RHIEC            Unreviewed;       569 AA.
AC   Q2K6H2;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 113.
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=degPch4 {ECO:0000313|EMBL:ABC91564.1};
GN   OrderedLocusNames=RHE_CH02795 {ECO:0000313|EMBL:ABC91564.1};
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834 {ECO:0000313|EMBL:ABC91564.1, ECO:0000313|Proteomes:UP000001936};
RN   [1] {ECO:0000313|EMBL:ABC91564.1, ECO:0000313|Proteomes:UP000001936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251 {ECO:0000313|Proteomes:UP000001936};
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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DR   EMBL; CP000133; ABC91564.1; -; Genomic_DNA.
DR   RefSeq; WP_011426041.1; NC_007761.1.
DR   AlphaFoldDB; Q2K6H2; -.
DR   KEGG; ret:RHE_CH02795; -.
DR   eggNOG; COG0265; Bacteria.
DR   HOGENOM; CLU_020120_1_0_5; -.
DR   OrthoDB; 9758917at2; -.
DR   Proteomes; UP000001936; Chromosome.
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; IPR041489; PDZ_6.
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; 1.
DR   Pfam; PF17820; PDZ_6; 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:ABC91564.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001936};
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..569
FT                   /note="Probable periplasmic serine endoprotease DegP-like"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039240501"
FT   DOMAIN          304..395
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          463..524
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          43..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          403..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..61
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        156
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT   ACT_SITE        186
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT   ACT_SITE        260
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ   SEQUENCE   569 AA;  58830 MW;  A855498F43BF11DE CRC64;
     MAPTIRLPFR RTLALLASAT ILAQTGMSGI AFAQTSPETA VPGVAAPVPA APTPPASTPQ
     QTPPVQTVVP TNGPASVADL AEGLLDAVVN ISTSQNVKDD EGVGPAPRAP DGSPFQEFFN
     DFFNKKQGNK GPNHNVSSLG SGFVIDPAGY IVTNNHVIEG ADDIEVNFAN GSKLKAKLIG
     TDTKTDLSVL KVEPKTPLKS VKFGDSSEMR IGDWVMAIGN PFGFGGSVTV GIISGRGRNI
     NAGPYDNFIQ TDAAINKGNS GGPLFNMKGE VIGINTAIIS PSGGSIGIGF SVPSELASGV
     VEQLRQYGET RRGWLGVRIQ PVTDDIADSL GLDTAKGALV AGVIKGGPVD DGSIKAGDVI
     LKFDGKTVNE MRDLPRVVAE STVGKEVDVV VLRDGKEQTV KVKLGRLEDS DQAASGDASP
     DGSQDGVITP DPDENDDMDQ PDTGDQVAPA PGAPAPDQHQ QGQVSPDAAT PKNVLGLSLS
     LLSPETRKAF GIAESVDGVV VTEVEPGSAS AEKGLKPGDV IVEVAQEFMK SPDAVAAKVK
     SLKQEGRRNA QLMIASANGD LRFVAVPME
//
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