ID A0A1U7DBJ9_9RHOB Unreviewed; 459 AA.
AC A0A1U7DBJ9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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};
DE Flags: Precursor;
GN ORFNames=Ga0080559_TMP4650 {ECO:0000313|EMBL:APX25446.1};
OS Salipiger profundus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=1229727 {ECO:0000313|EMBL:APX25446.1, ECO:0000313|Proteomes:UP000186559};
RN [1] {ECO:0000313|EMBL:APX25446.1, ECO:0000313|Proteomes:UP000186559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLT2016 {ECO:0000313|EMBL:APX25446.1,
RC ECO:0000313|Proteomes:UP000186559};
RA Tang K.;
RT "Deep-sea bacteria in the southern Pacific.";
RL Submitted (MAR-2016) 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}.
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DR EMBL; CP014796; APX25446.1; -; Genomic_DNA.
DR RefSeq; WP_076625009.1; NZ_CP014796.1.
DR AlphaFoldDB; A0A1U7DBJ9; -.
DR STRING; 1229727.Ga0080559_TMP4650; -.
DR KEGG; tpro:Ga0080559_TMP4650; -.
DR Proteomes; UP000186559; Chromosome.
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.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:APX25446.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:APX25446.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186559};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..459
FT /note="Probable periplasmic serine endoprotease DegP-like"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038379745"
FT DOMAIN 255..346
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 363..450
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 106
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 136
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 210
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 459 AA; 47768 MW; 9493444D76BC3357 CRC64;
MLSRLTFLFV LSICVVARPA VAQIAAVEPD ERGIPTIAPL IDAVDDAVVN IAVVSERPAQ
MTPLFRDPYF QPFLPPLEQL PPQRQMSAGS GVIVDAGEGY ILTNNHVVEN GDEIRVTLRD
NRTIEAELIG RDPATDIAVL RIDANNLTEV PLGDSETLLV GDFVVAIGNP FGLGQTVTSG
IVSALGRSGI NPEGYEDFIQ TDASINPGNS GGALITLDGN LVGINTAIIA PNGGGNVGIG
FAVPINMALA VMDQLVEFGE VQRGRLGVMI QDLTPDLAEA LGADAEAGAI VSSVEPGTPA
DDAGLIPGDV IVAVDGEGVD GSADLRQRIG LHRPGDEVEI TYVRDGDRLV TQVALADGGG
PRLAERDRGT SDALAGVHLA PLDRHHPAWG DADGVVVSEI APGSRAAQAG LEAGDVITAV
NRQTVGSIRD IDRVLADAPN AVALTVWRDG RTLLIVLRS
//
