ID K7ZAU3_BDEBC Unreviewed; 191 AA.
AC K7ZAU3;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Intracellular protease containing a glutamine amidotransferase domain {ECO:0000313|EMBL:AFY01889.1};
GN ORFNames=Bdt_2204 {ECO:0000313|EMBL:AFY01889.1};
OS Bdellovibrio bacteriovorus str. Tiberius.
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=1069642 {ECO:0000313|EMBL:AFY01889.1, ECO:0000313|Proteomes:UP000010074};
RN [1] {ECO:0000313|EMBL:AFY01889.1, ECO:0000313|Proteomes:UP000010074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tiberius {ECO:0000313|EMBL:AFY01889.1,
RC ECO:0000313|Proteomes:UP000010074};
RX PubMed=23181807; DOI=10.1186/1471-2164-13-670;
RA Hobley L., Lerner T.R., Williams L.E., Lambert C., Till R., Milner D.S.,
RA Basford S.M., Capeness M.J., Fenton A.K., Atterbury R.J., Harris M.A.,
RA Sockett R.E.;
RT "Genome analysis of a simultaneously predatory and prey-independent, novel
RT Bdellovibrio bacteriovorus from the River Tiber, supports in silico
RT predictions of both ancient and recent lateral gene transfer from diverse
RT bacteria.";
RL BMC Genomics 13:670-670(2012).
CC -!- SIMILARITY: Belongs to the peptidase C56 family.
CC {ECO:0000256|ARBA:ARBA00008542}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002930; AFY01889.1; -; Genomic_DNA.
DR RefSeq; WP_015091329.1; NC_019567.1.
DR AlphaFoldDB; K7ZAU3; -.
DR STRING; 1069642.Bdt_2204; -.
DR KEGG; bbat:Bdt_2204; -.
DR PATRIC; fig|1069642.3.peg.2181; -.
DR HOGENOM; CLU_000445_44_4_7; -.
DR Proteomes; UP000010074; Chromosome.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03134; GATase1_PfpI_like; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR006286; C56_PfpI-like.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR002818; DJ-1/PfpI.
DR NCBIfam; TIGR01382; PfpI; 1.
DR PANTHER; PTHR42733; DJ-1 PROTEIN; 1.
DR PANTHER; PTHR42733:SF12; PROTEIN_NUCLEIC ACID DEGLYCASE 2; 1.
DR Pfam; PF01965; DJ-1_PfpI; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51276; PEPTIDASE_C56_PFPI; 1.
PE 3: Inferred from homology;
KW Glutamine amidotransferase {ECO:0000313|EMBL:AFY01889.1};
KW Hydrolase {ECO:0000313|EMBL:AFY01889.1};
KW Protease {ECO:0000313|EMBL:AFY01889.1};
KW Transferase {ECO:0000313|EMBL:AFY01889.1}.
FT DOMAIN 8..175
FT /note="DJ-1/PfpI"
FT /evidence="ECO:0000259|Pfam:PF01965"
SQ SEQUENCE 191 AA; 21000 MW; 7EC537EF33828CFF CRC64;
MTQSLSGKKI AIIATDGFEE SELVEPRNYL DKAGAQTVLV SLKPGHIKAW KKGEWGDFLA
VDKSLDEVDP SEFDALMIPG GVINPDKLRM DKKAVKFVQA FVDSHKPIAA ICHGPQLLIE
TGIVSGRKIT SWPSLRTDLI NAGGDWFDTQ VMVDQGLVTS RKPEDISAFS EKMIEVFSMG
DQQMKDTLPP L
//
