ID A0A328AJ82_9CAUL Unreviewed; 525 AA.
AC A0A328AJ82;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=DJ017_08150 {ECO:0000313|EMBL:RAK54495.1};
OS Phenylobacterium soli.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=2170551 {ECO:0000313|EMBL:RAK54495.1, ECO:0000313|Proteomes:UP000249254};
RN [1] {ECO:0000313|Proteomes:UP000249254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LX32 {ECO:0000313|Proteomes:UP000249254};
RA Li X.;
RL Submitted (MAY-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:RAK54495.1}.
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DR EMBL; QFYQ01000001; RAK54495.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A328AJ82; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000249254; 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; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:RAK54495.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000249254};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..525
FT /note="Probable periplasmic serine endoprotease DegP-like"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038666534"
FT DOMAIN 296..387
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 95..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 150
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 180
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 252
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 525 AA; 53786 MW; 9BBEFB988A4993BE CRC64;
MTSKKTGYLF GAIAGAGVMA AAVAGAGIRL PAAHPGDGQV IKASTAPIFA PPPGAPMSFA
DIFEKVSPAV VSINVTSRVD PSLLRRIPGL EGLPFDIVPK GGQGGDDDEG GATPPKGGRT
EKGQPKLPTQ QSSGSGFFIS PDGYIVTNNH VVENAETIKV VLKDERELDA KVVGRDEATD
LAVIKVTGGP FPFVNFENSA RPRVGDWVIA VGNPFGLGGT ATAGIVSAYG RDIGETFVDY
IQIDAPINRG NSGGPTFDIY GRVIGVNTAI FSPTGGSVGI GFAIPADVAE QVTQQLIRGG
KIQRGYIGAT IQNFTSEMAE AQGLGDQKGA IVSDLVPNGP SAKAGLLPGD VVVSVNGRSV
KSSSELTREV AKGRPGDVLR LDVIRDGRHR TVEVHSGVRP SEAELAANDN GQRGQGGGGA
TPQAPAAPAV LGLKLAPLDD ATRRQLGLPA EVRGAAVLSV DESSDAGEKG LKRGDVIVRA
GDRAVTSAAD VAAVVDQAKK AGRPSVLVGV YRGGRTLFLP LKISK
//
