ID S6ACW5_PSERE Unreviewed; 389 AA.
AC S6ACW5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=algW {ECO:0000313|EMBL:BAN46777.1};
GN ORFNames=PCA10_10450 {ECO:0000313|EMBL:BAN46777.1};
OS Pseudomonas resinovorans NBRC 106553.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1245471 {ECO:0000313|EMBL:BAN46777.1, ECO:0000313|Proteomes:UP000015503};
RN [1] {ECO:0000313|EMBL:BAN46777.1, ECO:0000313|Proteomes:UP000015503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 106553 {ECO:0000313|EMBL:BAN46777.1,
RC ECO:0000313|Proteomes:UP000015503};
RX PubMed=23887915; DOI=10.1128/genomeA.00488-13;
RA Shintani M., Hosoyama A., Ohji S., Tsuchikane K., Takarada H., Yamazoe A.,
RA Fujita N., Nojiri H.;
RT "Complete Genome Sequence of the Carbazole Degrader Pseudomonas
RT resinovorans Strain CA10 (NBRC 106553).";
RL Genome Announc. 1:e00488-13(2013).
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};
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DR EMBL; AP013068; BAN46777.1; -; Genomic_DNA.
DR RefSeq; WP_016490979.1; NC_021499.1.
DR AlphaFoldDB; S6ACW5; -.
DR STRING; 1245471.PCA10_10450; -.
DR MEROPS; S01.477; -.
DR KEGG; pre:PCA10_10450; -.
DR PATRIC; fig|1245471.3.peg.1056; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_2_6; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000015503; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-KW.
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; 1.
DR Gene3D; 2.30.42.10; -; 1.
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; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:BAN46777.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015503};
KW Stress response {ECO:0000256|ARBA:ARBA00023016};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 279..362
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 368..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 389 AA; 41328 MW; 1E16A586FA4907D6 CRC64;
MLKALRYFGW PLVVGVLAAL LIIQHYPQWV GLPQQEVHLQ EAPKFNFSRQ GPDSYADAVT
SASPAVANLY TTKMVSKPAH PLFEDPQFRR FFGDNLPRQR RMESSLGSAV IMSPEGYLLT
NNHVTAGADQ IVVALKDGRE TLAHLVGSDP ETDLAVLKID LKDLPSITLG RSDNIRIGDV
ALAIGNPFGV GQTVTMGIIS ATGRNQLGLN TYEDFIQTDA AINPGNSGGA LVDASGNLIG
INTAILSKSG GSQGIGFAIP TKLALEVMKA IIEHGSVIRG WLGIEVQPLT QELAESFGLE
GRPGIVVAGI YRDSPAQRAS LQPGDIILSI DGEPAGDGRR SMNQVARTRP SEKISILVMR
NGKELELTAE VGVRPPPSNN GSNGGNGSN
//
