ID A0A257J9U6_9PROT Unreviewed; 471 AA.
AC A0A257J9U6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=CFE28_11885 {ECO:0000313|EMBL:OYU71689.1};
OS Alphaproteobacteria bacterium PA2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=2015570 {ECO:0000313|EMBL:OYU71689.1, ECO:0000313|Proteomes:UP000215921};
RN [1] {ECO:0000313|EMBL:OYU71689.1, ECO:0000313|Proteomes:UP000215921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA2 {ECO:0000313|EMBL:OYU71689.1};
RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT formosa and its bacterial cohort.";
RL Submitted (JUN-2017) 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 -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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:OYU71689.1}.
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DR EMBL; NKIZ01000001; OYU71689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257J9U6; -.
DR Proteomes; UP000215921; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:OYU71689.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000215921};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 282..340
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 387..441
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 110
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 140
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 217
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 471 AA; 48600 MW; 869AA8C470EBB539 CRC64;
MRAYRVLIPA IALLAACSDP SSRSSAQQPA LAQPTRAAPS EALTMKASFA PVVKRAAPAV
VNISSKRLVR TPNDPFWEFF GMGAPRNRIE GSLGSGVIVR SDGIIVTNNH VIQGGQEITV
ALSDRREFAA KVLLSDPRLD LAVLKIDAGS ERLPVLAIDD SGDAQVGDLV LAIGDPFGVG
QTVTNGIISA LDRTADPNGE AVTAYIQTDA AINPGNSGGA LVDMDGDLIG VNSFIVSRSG
SSSGVGFAVP AAMVKRIVET AAGGGHTLVR SWLGAHTQTV TGEIAKSLGL PSPQGALVAD
IWPGGPADRA GLKQGDVITA VDDKPVIDAS TVSYAVGAVR PGDTVKLTYR RGDANRVVSF
RAEAPPATPA RDEQALSGRH PFDGATVVNL SPAVADELGL DPLLGKGVMV LKIGRGFALN
AGLQPGDLIR KVNGRDIGSV SDLRSVLGAQ GGQWQVTIVR GGKEITGTFR T
//
