ID A0A1I7E101_9RHOB Unreviewed; 492 AA.
AC A0A1I7E101;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, 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=SAMN05216236_14029 {ECO:0000313|EMBL:SFU17608.1};
OS Sedimentitalea nanhaiensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Sedimentitalea.
OX NCBI_TaxID=999627 {ECO:0000313|EMBL:SFU17608.1, ECO:0000313|Proteomes:UP000182466};
RN [1] {ECO:0000313|EMBL:SFU17608.1, ECO:0000313|Proteomes:UP000182466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10959 {ECO:0000313|EMBL:SFU17608.1,
RC ECO:0000313|Proteomes:UP000182466};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FPAW01000040; SFU17608.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7E101; -.
DR STRING; 999627.SAMN05216236_14029; -.
DR eggNOG; COG0265; Bacteria.
DR Proteomes; UP000182466; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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; 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:SF130; PERIPLASMIC SERINE ENDOPROTEASE DEGP-LIKE; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 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; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SFU17608.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000182466};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 272..347
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 125
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 155
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 228
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 492 AA; 52193 MW; 915BD712BD8168C1 CRC64;
MQPQAIAIKA PGPQIDQGRM RLFWVGALTI MFVLAQTLIA QAKPESLAPL AEKISPSVVN
ITTSTTIEGR TGPQGIVPDG SPFEDFFREF QDRNNNGDGP RPRRSSALGS GFVISEDGYV
VTNNHVIEGA DEILIEFFAG GELPAKVVGT DPNTDIALLK VESDKPLPFV TFGDSDLARV
GDWVIAMGNP LGQGFSVSAG IVSARNRALS GTYDDYIQTD AAINRGNSGG PLFNMDGEVV
GVNTAILSPN GGSIGIGFSM ASNVVTRVVD QLKEFGETRR GWLGVRIQDV TDEIAEAMGL
ESTAGALITD VPEGPAMEAG LLSGDVIVSF DGVEVADTRA LVRQVGNTTV GKAVRVVINR
EGNRKTVLVT LGRREEAEGA VPAAMEKSDP EMQEKTVLGM TLSLLNDQLR SEMGLSETQT
GLVVLSVDET SEAFEKGLRA GDLITEAGQQ KVTALDQLDD RIAEARDAGR KSLLLLVRRG
GDPRFVALGL DD
//
