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Database: UniProt
Entry: Q2N7I1_ERYLH
LinkDB: Q2N7I1_ERYLH
Original site: Q2N7I1_ERYLH 
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
//
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