ID A0A0N1LPV9_9PROT Unreviewed; 511 AA.
AC A0A0N1LPV9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=IP70_00815 {ECO:0000313|EMBL:KPF88219.1};
OS alpha proteobacterium AAP38.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1523418 {ECO:0000313|EMBL:KPF88219.1, ECO:0000313|Proteomes:UP000037884};
RN [1] {ECO:0000313|EMBL:KPF88219.1, ECO:0000313|Proteomes:UP000037884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP38 {ECO:0000313|EMBL:KPF88219.1,
RC ECO:0000313|Proteomes:UP000037884};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) 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:KPF88219.1}.
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DR EMBL; LJHR01000003; KPF88219.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1LPV9; -.
DR STRING; 1523418.IP70_00815; -.
DR PATRIC; fig|1523418.3.peg.2095; -.
DR Proteomes; UP000037884; 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:KPF88219.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 288..349
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 415..497
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 390..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 133
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 165
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 239
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 511 AA; 53296 MW; DCF9AAF43DE85244 CRC64;
MDAFRSRSAR ATAGAVVREG RVAGLLSLLA VTAALIFTPP ALAQRGAPDS FAPLAEKTLP
SVVNISTSQT IQNKQGGRGA VPMPDFPPGS PMEEFFRDFL ERQQQGQGAP RKAQSLGSGF
IIDASGYIVT NNHVIEGADE ITVIFQDADQ TELKAKLIGT DKETDLALLK VETKQKLTAL
KWGDSDVLKV GDWVVAIGNP FGLGGTVTAG IVSARARDIG AGRFDDFIQT DAAINQGNSG
GPLVNLAGDV VGINSAIYSR TGGSVGIGFA IPSSMARTVI EEIRKAGKVR RGWLGVQIQS
VTPEIAESMG LAHHKGALVG TVTEGSPAAA AGLKPGDVIL TFDGKEVANN RTLPRMVAGT
PVGTKVNVGI SRKGTPVNVT VALAEFPEEP AAAEEEQPEE QQSGTSGAQQ QVDALGLTVS
AITAELRKQF ELAEGTKGVV ITKVNPNAPA QSRQLRPGDV VLEVSQQPVT TPADVQDRVG
KAKTAGQKAV LLLVERRGEQ TFLALSLEGA P
//
