ID A0A0J9H422_9RHOB Unreviewed; 507 AA.
AC A0A0J9H422;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 ORFNames=AIOL_000609 {ECO:0000313|EMBL:KMW60453.1};
OS Candidatus Rhodobacter lobularis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1675527 {ECO:0000313|EMBL:KMW60453.1, ECO:0000313|Proteomes:UP000037178};
RN [1] {ECO:0000313|EMBL:KMW60453.1, ECO:0000313|Proteomes:UP000037178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IGS {ECO:0000313|EMBL:KMW60453.1};
RA Jourda C., Santini S., Claverie J.-M.;
RT "Draft genome sequence of an Alphaproteobacteria species associated to the
RT Mediterranean sponge Oscarella lobularis.";
RL Submitted (JUN-2015) 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:KMW60453.1}.
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DR EMBL; LFTY01000001; KMW60453.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J9H422; -.
DR STRING; 1675527.AIOL_000609; -.
DR PATRIC; fig|1675527.3.peg.666; -.
DR Proteomes; UP000037178; 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; PF13180; PDZ_2; 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};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KMW60453.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037178};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 287..377
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 383..495
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 140
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 170
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 243
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 507 AA; 53641 MW; 0CA270184B77B183 CRC64;
MRTPALIAIA GATEWRENVT PQALPIPAQP PLQLRALWAA LMGLAILIAQ STMAPAQSRP
DSFADLAETI SPSVVNITTA TNVAASTTPE LSVPDGSPFE DFFRDFMDRN QDNPRRPRRS
SALGSGFVIS ADGFIVTNNH VIEGADEITI EFFSGEERDA TLIGRDPNTD IALLKVEVDA
PLEFVEFGDS DGARVGDWVM AMGNPLGQGF SVSVGIISAR NRALSGSYDD YIQTDAAINR
GNSGGPLFNM DGDVIGVNTA ILSPNGGSIG IGFSMASNVV TKVVDQLQEF GETRRGWLGV
RIQDVDEDTA EALGLVKASG ALVTDVPDGP AKQAGIESGD VIMTFDGTEV EDTRQLVRVV
GATAVGKAVD VIIFRGGEEV TLSVTLGRRE EAEGAIPATA PAAPEEPVEK DVLGLTVTGM
SDELRQQLGL AEDAEGLVVR EVDETAQAYE KGLRAGDVIT EAGQQKVNVV TDLEDRIAEA
KDAGRKSLLL LVRRNGEPRF VALTLDG
//
