ID A0A142Y9W5_9PLAN Unreviewed; 520 AA.
AC A0A142Y9W5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, 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 Name=degP_1 {ECO:0000313|EMBL:AMV35999.1};
GN ORFNames=VT85_01045 {ECO:0000313|EMBL:AMV35999.1};
OS Planctomyces sp. SH-PL62.
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC Planctomycetaceae; Planctomyces.
OX NCBI_TaxID=1636152 {ECO:0000313|EMBL:AMV35999.1, ECO:0000313|Proteomes:UP000076365};
RN [1] {ECO:0000313|EMBL:AMV35999.1, ECO:0000313|Proteomes:UP000076365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH-PL62 {ECO:0000313|EMBL:AMV35999.1,
RC ECO:0000313|Proteomes:UP000076365};
RA van der Voort M., Raaijmakers J.M.;
RT "Genome minning of novel planctomycete species.";
RL Submitted (APR-2015) 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}.
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DR EMBL; CP011273; AMV35999.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A142Y9W5; -.
DR STRING; 1636152.VT85_01045; -.
DR KEGG; plh:VT85_01045; -.
DR OrthoDB; 248175at2; -.
DR Proteomes; UP000076365; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 1.
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; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
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, ECO:0000313|EMBL:AMV35999.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:AMV35999.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076365};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 295..360
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 520 AA; 54490 MW; 121221013BD00409 CRC64;
MASYNVTDDG YGYDAPPPRP TTPPVRRGFV MILALLSLAV LAVYGVPFIA ERAGRAWEAG
RAQAASAALS KLDEQGAVSQ ASRLFRLATT AVSPAVVNVR SFRGSSGIGR HGLPIGGPPS
DREGLRSELG SGVVIDKVNG YIVTNNHVIQ DAEEIIVRLG PRDDVPARLV GADPKTDLAV
LQVRTELKTA AEWGDSDKLD IGDWVLAIGS PLGFDHSVTA GIVSATERND LRIAEYESFI
QTDAAINPGN SGGPLIDLSG RIVGINTAII TQSGGYEGIG LAIPTSLARR VVEALIKDGR
VTRGFLGVAM QPLDDETAKL LKFPGKPDGV VVGGVIPDGP AARADLRPGD VIVSLDGRPV
HDPTGLRYVT ADLGAGIDVP VVFYREGAEQ KVTVTLAESP TNPEIAPLGF RVKEVDAPTP
DGKPRTIVEV DRVVSAGPAF NAGLRPGMWI AAVDQTQVHS VLQFLALIRN YDLEHRLPLF
VVTPDGRGAG LVILGPKAVQ DQPPGQAAEG LGPPSATEGP
//
