ID A0A1I3H2B0_9BRAD Unreviewed; 467 AA.
AC A0A1I3H2B0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN05216525_10710 {ECO:0000313|EMBL:SFI29864.1};
OS Bradyrhizobium sp. Gha.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1855318 {ECO:0000313|EMBL:SFI29864.1, ECO:0000313|Proteomes:UP000199284};
RN [1] {ECO:0000313|EMBL:SFI29864.1, ECO:0000313|Proteomes:UP000199284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gha {ECO:0000313|EMBL:SFI29864.1,
RC ECO:0000313|Proteomes:UP000199284};
RA de Groot N.N.;
RL Submitted (OCT-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};
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DR EMBL; FOQM01000007; SFI29864.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3H2B0; -.
DR STRING; 1855318.SAMN05216525_10710; -.
DR Proteomes; UP000199284; 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:SFI29864.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..467
FT /note="Probable periplasmic serine endoprotease DegP-like"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039253090"
FT DOMAIN 252..350
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 402..444
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 108
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 138
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 214
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 467 AA; 49279 MW; 80CDC1F44DB3BDC5 CRC64;
MFRANLTAVV TALCMAFSAH FNPAAAQDRR VPSSPAELRL SYAPIVQRVQ PAVVNVYAAK
VVQNRNPLLD DPIFRRFFGG GEQQEQVQRS LGSGVIVDSS GLIVTNVHVI EGADQVKVSL
ADKREFEAEI VLKDSRSDLA VLRLKDTKEK FPALEFTNSD ELMVGDVVLA IGNPFGVGQT
VTHGIISALA RTQVGITDYQ FFIQTDAPIN PGNSGGALVD MNGRLAGINT AIYSRSGGSQ
GIGFAIPANM VRVVVASAKS GGTAVKRPWL GAKLQAVTAE IAESLGLRSP TGALVASVVP
NGPAAKAGLK SSDLITGIDG QAVDDPNAFD YRFATRPLGG TAQIDVQRGS KPLKLTIALE
TAPDSGRNEL VITTRSPFQG ARISTITPAV ADELHLDVDT EGVVVTDIGD GTAAQNVGFQ
KGDIILSVNS QKIIRTSDLE KAAKEQPRLW RIALVRGGQQ INVTLGG
//
