ID A0A0B2BZI0_9SPHN Unreviewed; 508 AA.
AC A0A0B2BZI0;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=PK98_08070 {ECO:0000313|EMBL:KHL26849.1};
OS Croceibacterium mercuriale.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Croceibacterium.
OX NCBI_TaxID=1572751 {ECO:0000313|EMBL:KHL26849.1, ECO:0000313|Proteomes:UP000030988};
RN [1] {ECO:0000313|EMBL:KHL26849.1, ECO:0000313|Proteomes:UP000030988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Coronado {ECO:0000313|EMBL:KHL26849.1,
RC ECO:0000313|Proteomes:UP000030988};
RA Coil D.A., Eisen J.A.;
RT "Draft genome sequence of Kirrobacter mercurialis.";
RL Submitted (NOV-2014) 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};
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:KHL26849.1}.
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DR EMBL; JTDN01000001; KHL26849.1; -; Genomic_DNA.
DR RefSeq; WP_039096465.1; NZ_JTDN01000001.1.
DR AlphaFoldDB; A0A0B2BZI0; -.
DR STRING; 1572751.PK98_08070; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000030988; 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:SF130; PERIPLASMIC SERINE ENDOPROTEASE DEGP-LIKE; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR Pfam; PF13180; PDZ_2; 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; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KHL26849.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030988};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..508
FT /note="Probable periplasmic serine endoprotease DegP-like"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038617208"
FT DOMAIN 285..346
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 118
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 154
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 229
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 508 AA; 52775 MW; 20E7710FC34FE8E6 CRC64;
MRYSYGITAA LLAGAASLSL ITGFPAGAQV AQNDAGAMTN MVPRAGAPAS FADLTEQLQP
AVVNISTRQR VTVTNNPFAG TPFEGMFGNQ GQQSTREAQS LGSGFIISAD GYVVTNNHVI
SPPDTNAELE EVTVTLPDGK EYQAEVVGND ADSDLAVLKI VRDEPFPFVK FGDSAAARAG
DWVVAIGNPF GLGGTVTSGI ISSVLRSGLN GGAYDRYIQT DASINRGNSG GPLFDMQGNV
IGINNAIFSP SGGSVGIGFA IPADTAAPIV RQLIAGEEIV RGYLGVQIQP MNEDLAAALG
IAANRGEFIQ GVQPGEAAEQ AGLQAGDVVL TVDGKEVTPE QSLSFLVANT APGTRIPLEI
IREGQRRTIQ VAVGRRPSAE ELQAQQFSMD EEAPEQQQPL PSSDGLIPQA LGLQVTPITP
LIARQLGVGN DTRGLVVLAV DQSADAARKG LRRGVIIETV NGSPVATTGD LEAAIRAARG
ENREAILLRV RARGGPATSL PIRLRAAQ
//
