ID A0A2T7FY78_9RHOB Unreviewed; 467 AA.
AC A0A2T7FY78;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=DC363_07455 {ECO:0000313|EMBL:PVA07119.1};
OS Thalassorhabdomicrobium marinisediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thalassorhabdomicrobium.
OX NCBI_TaxID=2170577 {ECO:0000313|EMBL:PVA07119.1, ECO:0000313|Proteomes:UP000244817};
RN [1] {ECO:0000313|EMBL:PVA07119.1, ECO:0000313|Proteomes:UP000244817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH-SD16 {ECO:0000313|EMBL:PVA07119.1,
RC ECO:0000313|Proteomes:UP000244817};
RA Ji X.;
RT "Pelagivirga bohaiensis gen. nov., sp. nov., a bacterium isolated from the
RT Bohai Sea.";
RL Submitted (APR-2018) 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:PVA07119.1}.
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DR EMBL; QCYG01000004; PVA07119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7FY78; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000244817; 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:PVA07119.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244817};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..467
FT /note="Probable periplasmic serine endoprotease DegP-like"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039582568"
FT DOMAIN 248..326
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 345..456
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 94
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 129
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 204
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 467 AA; 48561 MW; 20AAC3DBC8430309 CRC64;
MLGAFLALVS ILPAAAQNRP DTFADLAEQV SPAVVNITTS TVVANRTGPR GIVPEGSPFE
DFFNDFNNGQ PRRSSALGSG FVISADGYIV TNNHVIEGAD EIEIEFFPGA GQPADLLPAE
LVGTDPNTDI AVLKVDYDAP LKFVSFGDSD ADGARVGDWV LAMGNPLGQG FSVSAGIVSA
RNRSLQGTYD DYIQTDAAIN RGNSGGPLFN MDGEVIGVNT AILSPNGGSI GIGFAMSSAV
VTNVVDQLKE FGETRRGWLG VRIQDVTPDM VEAIDGLSAA RGAMVTDVPT GPAEEAGVEA
GDVILTFDGV EVADTRELVQ IVGNSPVGKA VPVEILRNGD VINVTVTLGR RETSEASAFP
GDVPAPGQPE TTNMLGLTLS EITPDIAEEL GVNANAGLVV VEVEIGSDAE GKGLRAGDVI
TEAGQQKITN ISDFETRVEE AQEAGRKSVL LLVRRGGAPR FVALSLE
//
