ID Q2N7I1_ERYLH Unreviewed; 510 AA.
AC Q2N7I1;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 24-JAN-2024, entry version 108.
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 OrderedLocusNames=ELI_11340 {ECO:0000313|EMBL:ABC64360.1};
OS Erythrobacter litoralis (strain HTCC2594).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=314225 {ECO:0000313|EMBL:ABC64360.1, ECO:0000313|Proteomes:UP000008808};
RN [1] {ECO:0000313|Proteomes:UP000008808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2594 {ECO:0000313|Proteomes:UP000008808};
RX PubMed=19168610; DOI=10.1128/JB.00026-09;
RA Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.;
RT "Complete genome sequence of Erythrobacter litoralis HTCC2594.";
RL J. Bacteriol. 191:2419-2420(2009).
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}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; CP000157; ABC64360.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2N7I1; -.
DR STRING; 314225.ELI_11340; -.
DR KEGG; eli:ELI_11340; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_0_5; -.
DR OMA; GPAFDTN; -.
DR Proteomes; UP000008808; 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; 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; 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; 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; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:ABC64360.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008808};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 275..351
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 382..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
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 510 AA; 54150 MW; FE9FCE0EC54E57C3 CRC64;
MKPVRYAYGL TSALLVGGAT VSLLTGQPAG AQVAQNDDRV MSNVVPRAGA PESFAELTEQ
LQPAVVNIST RQRIEVQNRN PFQGTPFADL FNRRGQPQQP QTREAQSLGS GFFISADGYV
VTNNHVVAPN GRGTVEEITV TLPDGREYAA ELVGADAASD LAVLKVSRSE PFPFVRFGDS
SQARAGDWVI AIGNPFGLGG TVTSGIVSAQ LRNTGGGAYD RYIQTDASIN RGNSGGPLFD
MQGNVIGINN AIFSPSGGSV GIGFAIPAET AAPIVAQLQR GNAIERGYLG VQIQQVSEDV
ADSLGLPKNR GEIVQTVVDG EAADRSGIRA GDVVLKIDGK DVTPDQTLSF LIANISPGTT
VPVEVFREGS RRTLNVTVGK RPSEEELRQS QIFSQDEDED PDAAPEMDDS EMLADKLGLG
VIPVTPEIAR QLGVAADTRG LAIAVVDPNS DAARKGLRRR DIILSANYEP VESVEDLEAI
VQQAEEAGRS SVLLRFRRGG QTAFRAVRFR
//