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Database: UniProt
Entry: D9QFU3_BRESC
LinkDB: D9QFU3_BRESC
Original site: D9QFU3_BRESC 
ID   D9QFU3_BRESC            Unreviewed;       416 AA.
AC   D9QFU3;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Peptidase M20 {ECO:0000313|EMBL:ADL00657.1};
GN   OrderedLocusNames=Bresu_1345 {ECO:0000313|EMBL:ADL00657.1};
OS   Brevundimonas subvibrioides (strain ATCC 15264 / DSM 4735 / LMG 14903 /
OS   NBRC 16000 / CB 81) (Caulobacter subvibrioides).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=633149 {ECO:0000313|EMBL:ADL00657.1, ECO:0000313|Proteomes:UP000002696};
RN   [1] {ECO:0000313|Proteomes:UP000002696}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15264 / DSM 4735 / LMG 14903 / NBRC 16000 / CB 81
RC   {ECO:0000313|Proteomes:UP000002696};
RX   PubMed=21705585; DOI=10.1128/JB.05453-11;
RG   US DOE Joint Genome Institute;
RA   Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL   J. Bacteriol. 193:4567-4568(2011).
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DR   EMBL; CP002102; ADL00657.1; -; Genomic_DNA.
DR   RefSeq; WP_013268760.1; NC_014375.1.
DR   AlphaFoldDB; D9QFU3; -.
DR   STRING; 633149.Bresu_1345; -.
DR   KEGG; bsb:Bresu_1345; -.
DR   eggNOG; COG0624; Bacteria.
DR   HOGENOM; CLU_021802_7_0_5; -.
DR   InParanoid; D9QFU3; -.
DR   OrthoDB; 9776600at2; -.
DR   BioCyc; BSUB633149:G1GM8-1339-MONOMER; -.
DR   Proteomes; UP000002696; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF9; BLL0789 PROTEIN; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002696}.
FT   DOMAIN          201..297
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   416 AA;  43342 MW;  2B75A318D6B7D4CF CRC64;
     MRILPQDHAA LDLVGRGEAI LIDRAVAWSN VNSGSDNPDG LNAMLDLLEA EAARLPAEVI
     RVQTQGFSTV ADDGTVRPQS RADALKVTAR PDAPIQVVLT GHYDTVYPAD SAFQTVAHRL
     DGALNGPGIA DMKGGISVML GALEAFETHP DRANVGWTVL LSPDEEIGSP ASAPLLAELG
     ARGHVGMTYE PALADGTLAG ARKGSGNFHL IVRGRAAHAG RAFHEGANAV AGAAIVAAAL
     HGLNGRREGV TVNVARISGG GALNVVADNA VVRFNVRVPD AQAAAWITDA IAEIAATPPF
     DGLMLDLHGG MTRAPKPMDA SQTALFEAVR ETGALLGQTI AWSPSGGVCE GNNLHAAGLP
     NIDTLGVRGG LIHSPEEFAW PESFVERARL STLMLCKIAS GEIDAQRLKR LRLETL
//
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