ID A0A011QQK7_9PROT Unreviewed; 509 AA.
AC A0A011QQK7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
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_4 {ECO:0000313|EMBL:EXI81184.1};
GN ORFNames=AW12_02802 {ECO:0000313|EMBL:EXI81184.1};
OS Candidatus Accumulibacter sp. BA-94.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=1454005 {ECO:0000313|EMBL:EXI81184.1, ECO:0000313|Proteomes:UP000020878};
RN [1] {ECO:0000313|EMBL:EXI81184.1, ECO:0000313|Proteomes:UP000020878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA-94 {ECO:0000313|Proteomes:UP000020878};
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:EXI81184.1}.
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DR EMBL; JEMZ01000195; EXI81184.1; -; Genomic_DNA.
DR STRING; 1454005.AW12_02802; -.
DR PATRIC; fig|1454005.3.peg.2732; -.
DR Proteomes; UP000020878; 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:EXI81184.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:EXI81184.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000020878};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 285..346
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 133
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 163
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 236
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 509 AA; 54711 MW; BFF13249696E2A40 CRC64;
MHSSTLDANP VNTDLNQETA GAMKRFLLAF FFVLFSLPAQ SQNRGLPDFT ELVEKQGPAV
VNISTTQTQR SGGKGAQPFP FDENDPMYEF FRRFIPRQPG MPGLPGVPRE FESRSLGSGF
VISADGYILT NAHVVESADE ILVRLTDKRE FKARVIGTDK RTDVALIKIE ANGLPTVRLG
DPGVLKVGEW VVAIGSPFGF DNSVTAGIVS AKGRSLPQEN FVPFLQTDVA VNPGNSGGPL
FNMRGEVVGI NSQIYSRSGG FMGISFAIPI DVAMEVQGQL RASGKVSRGR IGVVIQEVTK
ELAESFGLAK AQGAVVNAVE KGGPADKGGV EPGDVILKFD GKPITSSGDL PRIVGGTRPG
SKATIQVWRK GATRDLVLVV AEIPVEEKTA SRSXXXXXXS RSVKPAERAA NRLGLVVSEL
TAEQKRELRL DAGLLVEDVR NMATRTELRP GDIVLALIAR GESIELKSVE QFNRLLGQID
KSGSVTLLVR RGELQTFVTI KAAPEKRGE
//
