ID Q7VQR9_BLOFL Unreviewed; 461 AA.
AC Q7VQR9;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=peptidase Do {ECO:0000256|ARBA:ARBA00013035};
DE EC=3.4.21.107 {ECO:0000256|ARBA:ARBA00013035};
GN Name=degQ {ECO:0000313|EMBL:CAD83574.1};
GN OrderedLocusNames=Bfl047 {ECO:0000313|EMBL:CAD83574.1};
OS Blochmannia floridanus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Blochmannia.
OX NCBI_TaxID=203907 {ECO:0000313|EMBL:CAD83574.1, ECO:0000313|Proteomes:UP000002192};
RN [1] {ECO:0000313|EMBL:CAD83574.1, ECO:0000313|Proteomes:UP000002192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12886019; DOI=10.1073/pnas.1533499100;
RA Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F.,
RA Latorre A., Rausell C., Kramerbeek J., Gadau J., Hoelldobler B.,
RA van Ham R.C.H.J., Gross R., Moya A.;
RT "The genome sequence of Blochmannia floridanus: comparative analysis of
RT reduced genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003).
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};
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DR EMBL; BX248583; CAD83574.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7VQR9; -.
DR STRING; 203907.Bfl047; -.
DR KEGG; bfl:Bfl047; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_1_6; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000002192; Chromosome.
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:SF101; PERIPLASMIC PH-DEPENDENT SERINE ENDOPROTEASE DEGQ; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR Pfam; PF00595; PDZ; 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, ECO:0000313|EMBL:CAD83574.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:CAD83574.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 264..355
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 383..453
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 115
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 145
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 220
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 461 AA; 49037 MW; 9450D16AAC7FA1A6 CRC64;
MKIVNPIITI SIIFALICIN NLQTSNNYYT ALGSETPYLS MPTSLAPMLD NVLPTVVSIH
VEGTQPSKRL TLPKEFRYFF GPDLPNGNFG NRPFEGLGSG VIINSNKGYI ITNNHVVHGA
DKITIQLNDG REYNAKIIGH DEQTDLALLQ ILKFKNLSEI KIADSDTLKV GDFAVAIGNP
FGLGQTATSG IISALGRSGL NLEGLENFIQ TDASINRGNS GGALVNLNGE LIGINTAILA
PGGGNIGIGF AIPSNIVKNL SQQLIDFGEV KRGQLGIKGT ELTADIAKAF NIDIQRGAFV
SEVLPGSAAA KARIKAGDVI ISVEGKPIKN FAELRVKVGT TAPGKIIKIG LLRDGKTHIV
SVLLDDSTCV STSEENLIPA LQGATLSNNY LKDGTPGVQV EEINKDSPAA SIGLQKGDMI
IGLNRTRISN LSQLRKILKE NPTVMALNII RGGTNIFILL R
//
