Y1139_BURP1
ID Y1139_BURP1 Reviewed; 278 AA.
AC Q3JV52;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=UPF0758 protein BURPS1710b_1139;
GN OrderedLocusNames=BURPS1710b_1139;
OS Burkholderia pseudomallei (strain 1710b).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1710b;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
CC -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}.
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DR EMBL; CP000124; ABA48022.1; -; Genomic_DNA.
DR RefSeq; WP_004185928.1; NC_007434.1.
DR AlphaFoldDB; Q3JV52; -.
DR SMR; Q3JV52; -.
DR EnsemblBacteria; ABA48022; ABA48022; BURPS1710b_1139.
DR GeneID; 56594773; -.
DR KEGG; bpm:BURPS1710b_1139; -.
DR HOGENOM; CLU_073529_0_1_4; -.
DR OMA; AMPDYEL; -.
DR OrthoDB; 1833204at2; -.
DR Proteomes; UP000002700; Chromosome I.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd08071; MPN_DUF2466; 1.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR025657; RadC_JAB.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR001405; UPF0758.
DR InterPro; IPR020891; UPF0758_CS.
DR PANTHER; PTHR30471; PTHR30471; 1.
DR Pfam; PF04002; RadC; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR TIGRFAMs; TIGR00608; radc; 1.
DR PROSITE; PS50249; MPN; 1.
DR PROSITE; PS01302; UPF0758; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Zinc.
FT CHAIN 1..278
FT /note="UPF0758 protein BURPS1710b_1139"
FT /id="PRO_0000322676"
FT DOMAIN 156..278
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 227..240
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT COMPBIAS 32..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 278 AA; 29394 MW; 9E49AF1AA678D95D CRC64;
MQYEIVSAGE DVDDERARGR RAAAPAAPSS AVPSSAALSS AALSSAAQPT GAPPATAAAR
RGRDLPRERL LARGPAALSD AELVALLLGS GLPGHDVFAL AHTLLARFGS LRALLDAAPD
DFKGLRGIGP ARTAILVAVV ELARRALAEK ARERPLVDSP GAVDDYLRLL IGTRPREVFV
CLFLDARHRL VQTEETAHGS LTRMAVYPRE IVRRALALNA AALIVAHNHP SGAVRPSAAD
RRLTRVLRDA LALVDIKLID HFVVGASDTF SFAQAGWI
