ID E6BFT6_ECOLX Unreviewed; 455 AA.
AC E6BFT6;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=peptidase Do {ECO:0000256|ARBA:ARBA00013035};
DE EC=3.4.21.107 {ECO:0000256|ARBA:ARBA00013035};
GN Name=degQ {ECO:0000313|EMBL:EFU37126.1};
GN ORFNames=HMPREF9350_01192 {ECO:0000313|EMBL:EFU37126.1};
OS Escherichia coli MS 85-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=679202 {ECO:0000313|EMBL:EFU37126.1, ECO:0000313|Proteomes:UP000005056};
RN [1] {ECO:0000313|EMBL:EFU37126.1, ECO:0000313|Proteomes:UP000005056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS 85-1 {ECO:0000313|EMBL:EFU37126.1,
RC ECO:0000313|Proteomes:UP000005056};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2010) 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 -!- 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:EFU37126.1}.
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DR EMBL; ADWQ01000003; EFU37126.1; -; Genomic_DNA.
DR RefSeq; WP_001295271.1; NZ_ADWQ01000003.1.
DR AlphaFoldDB; E6BFT6; -.
DR SMR; E6BFT6; -.
DR MEROPS; S01.274; -.
DR GeneID; 75173402; -.
DR PATRIC; fig|679202.3.peg.1109; -.
DR Proteomes; UP000005056; Unassembled WGS sequence.
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; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR Pfam; PF00595; PDZ; 2.
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, ECO:0000313|EMBL:EFU37126.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:EFU37126.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..455
FT /note="peptidase Do"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039404545"
FT DOMAIN 258..349
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 355..447
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 109
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 139
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 214
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 455 AA; 47205 MW; 6A090F93AC021C83 CRC64;
MKKQTQLLSA LALSVGLTLS ASFQAVASIP GQVADQAPLP SLAPMLEKVL PAVVSVRVEG
TASQGQKIPE EFKKFFGDDL PDQPAQPFEG LGSGVIINAS KGYVLTNNHV INQAQKISIQ
LNDGREFDAK LIGSDDQSDI ALLQIQNPSK LTQIAIADSD KLRVGDFAVA VGNPFGLGQT
ATSGIVSALG RSGLNLEGLE NFIQTDASIN RGNSGGALLN LNGELIGINT AILAPGGGSV
GIGFAIPSNM ARTLAQQLID FGEIKRGLLG IKGTEMSADI AKAFNLDVQR GAFVSEVLPG
SGSAKAGVKA GDIITSLNGK PLNSFAELRS RIATTEPGTK VKLGLLRNGK PLEVEVTLDT
STSSSASAEM ITPALEGATL SDGQLKDGGK GIKIDEVVKG SPAAQAGLQK DDVIIGVNRD
RVNSIAEMRK VLAAKPAIIA LQIVRGNESI YLLMR
//
