ID A0A099GIM6_9RHOB Unreviewed; 509 AA.
AC A0A099GIM6;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=IX56_08050 {ECO:0000313|EMBL:KGJ22417.1};
OS Paracoccus sanguinis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1545044 {ECO:0000313|EMBL:KGJ22417.1, ECO:0000313|Proteomes:UP000029858};
RN [1] {ECO:0000313|EMBL:KGJ22417.1, ECO:0000313|Proteomes:UP000029858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5503 {ECO:0000313|EMBL:KGJ22417.1,
RC ECO:0000313|Proteomes:UP000029858};
RA McGinnis J.M., Wolfgang W.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGJ22417.1, ECO:0000313|Proteomes:UP000029858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5503 {ECO:0000313|EMBL:KGJ22417.1,
RC ECO:0000313|Proteomes:UP000029858};
RA Mingle L.A., Cole J.A., Lapierre P., Musser K.A.;
RT "Paracoccus sanguinis sp. nov., isolated from clinical specimens of New
RT York State patients.";
RL Submitted (OCT-2014) 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:KGJ22417.1}.
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DR EMBL; JRKQ01000033; KGJ22417.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099GIM6; -.
DR Proteomes; UP000029858; 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.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KGJ22417.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029858};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 297..378
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT DOMAIN 414..499
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 141
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 171
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 244
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 509 AA; 52273 MW; 258BE4E4A4352A17 CRC64;
MAPQDMPQTT TTPDQPMNGK VPEAANANAP IDVQKAPVAS GQSVMPDSFA DIVAQVSPAV
VNITTTAVVS RPVAQGPMFP EGSPFSDLFR DFGIPGVPGI PGGPDQGSPF GNRGPMQQER
SNALGSGFVV SADGFIVTNN HVIDGADEIE IEFYSGAKLP AKLVGTDPTT DIAVLKVEAE
KPLPFVKFGN SDSARVGDWV LALGNPLGQG LSASSGIISA KSRALTGTYD DFIQTDAAIN
RGNSGGPLFN MAGEVVGVNT AILSPNGGSI GIGFSMASNV VSKVVDQLRE FGETRRGWLG
VKIQDVTPDI AASLGLASET GAMVTDVPAG PAADAGVKAG DIITRFAGGD VADTRDLVRR
VADAPVGEAV DVTVQRAGQP VELKITLGRR ELADADGSGE GNDGAQPQGG DGRTVLGMTL
VPITPELAAR LRLPEGAKGL VVQDIDATSD ASAKGLQTGD VIVEAGQQPV TTLADLNARI
AEAKDAGRKS VLLLIRREGE PRFMALSIE
//
