ID G5LL64_SALET Unreviewed; 325 AA.
AC G5LL64;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=peptidase Do {ECO:0000256|ARBA:ARBA00013035};
DE EC=3.4.21.107 {ECO:0000256|ARBA:ARBA00013035};
DE Flags: Fragment;
GN ORFNames=LTSEALA_1194 {ECO:0000313|EMBL:EHC42856.1};
OS Salmonella enterica subsp. enterica serovar Alachua str. R6-377.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=913241 {ECO:0000313|EMBL:EHC42856.1, ECO:0000313|Proteomes:UP000004642};
RN [1] {ECO:0000313|EMBL:EHC42856.1, ECO:0000313|Proteomes:UP000004642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R6-377 {ECO:0000313|EMBL:EHC42856.1,
RC ECO:0000313|Proteomes:UP000004642};
RX PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA Furtado M.R., Wiedmann M.;
RT "Genome sequencing reveals diversification of virulence factor content and
RT possible host adaptation in distinct subpopulations of Salmonella
RT enterica.";
RL BMC Genomics 12:425-425(2011).
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:EHC42856.1}.
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DR EMBL; AFCJ01000526; EHC42856.1; -; Genomic_DNA.
DR AlphaFoldDB; G5LL64; -.
DR MEROPS; S01.274; -.
DR PATRIC; fig|913241.3.peg.921; -.
DR Proteomes; UP000004642; 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; 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; PF00595; PDZ; 1.
DR Pfam; PF13180; PDZ_2; 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:EHC42856.1}.
FT DOMAIN 128..219
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 225..317
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHC42856.1"
SQ SEQUENCE 325 AA; 33539 MW; CB7447AA39D815B2 CRC64;
SSGIALSLDI ALLQIQNPSK LTQIAIADSD KLRVGDFAVA VGNPFGLGQT ATSGIISALG
RSGLNLEGLE NFIQTDASIN RGNSGGALLN LNGELIGINT AILAPGGGSI GIGFAIPSNM
AQTLAQQLIQ FGEIKRGLLG IKGTEMTADI AKAFKLNVQR GAFVSEVLPN SGSAKAGVKS
GDVIISLNGK QLNSFAELRS RIATTEPGTK VKLGLLRDGK PLEVEVTLDS NTSSSASAEM
IAPALQGATL SDGQLKDGTK GVKVDSVEKS SPAAQAGLQK DDVIIGVNRD RISSIAEMRK
VMAAKPSIIA LQVVRGNENI YLLLR
//
