ID A0A011M7V0_9PROT Unreviewed; 481 AA.
AC A0A011M7V0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=mucD_3 {ECO:0000313|EMBL:EXI65768.1};
GN ORFNames=AW08_02980 {ECO:0000313|EMBL:EXI65768.1};
OS Candidatus Accumulibacter adjunctus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=1454001 {ECO:0000313|EMBL:EXI65768.1, ECO:0000313|Proteomes:UP000020218};
RN [1] {ECO:0000313|EMBL:EXI65768.1, ECO:0000313|Proteomes:UP000020218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-12 {ECO:0000313|Proteomes:UP000020218};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-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 -!- 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:EXI65768.1}.
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DR EMBL; JFAX01000019; EXI65768.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A011M7V0; -.
DR STRING; 1454001.AW08_02980; -.
DR PATRIC; fig|1454001.3.peg.3026; -.
DR Proteomes; UP000020218; 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; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.30.42.60; -; 1.
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, ECO:0000313|EMBL:EXI65768.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:EXI65768.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000020218};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..481
FT /note="Probable periplasmic serine endoprotease DegP-like"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038331214"
FT DOMAIN 263..324
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 111
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 141
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 214
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 481 AA; 51627 MW; C64D2745B4170624 CRC64;
MRQLLLAFFF VLFSLPAQAQ NRGLPDFTEL VEKQGPAVVN ISTTQTQRGG GRGAQPFPFD
ENDPMYEFFR RFIPRQPGMP GIPGMPREFE SRSLGSGFVI SADGYILTNA HVVESADEIL
VRLTDKREFK ARVIGTDKRT DVALIKIEAS GLPTVRLGDP GVLKVGEWVV AIGSPFGFDN
SVTAGIVSAK GRSLPQENFV PFIQTDVAVN PGNSGGPLFN MRGEVVGINS QIYSRSGGFM
GISFAIPIDV AMEVQGQLRA TGKVSRGRIG VVIQEVTKEL AESFGLAKAQ GAVVNAVEKG
GPADKAGVEP GDVILRFDGK PIAGSGDLPR IVGGTRPGSR ATIQVWRKGA TRDLVIVVAE
IPAEEKTAGR SSRSAKPAER AANRLGLVVA EPTPEQKREL KLDAGLLVED VRNMAARADL
RPGDILLALI ARGESIELKS VEQFNRLLAQ LDRSASVTLL VRRGELQTFV TIKAAPEKRG
E
//