Y2548_BURCM
ID Y2548_BURCM Reviewed; 258 AA.
AC Q0BCL9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=UPF0758 protein Bamb_2548;
GN OrderedLocusNames=Bamb_2548;
OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS (strain AMMD)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=339670;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-244 / AMMD;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA Ramette A., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}.
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DR EMBL; CP000440; ABI88104.1; -; Genomic_DNA.
DR RefSeq; WP_011657707.1; NZ_CP009798.1.
DR AlphaFoldDB; Q0BCL9; -.
DR SMR; Q0BCL9; -.
DR STRING; 339670.Bamb_2548; -.
DR EnsemblBacteria; ABI88104; ABI88104; Bamb_2548.
DR GeneID; 44693215; -.
DR GeneID; 60996092; -.
DR KEGG; bam:Bamb_2548; -.
DR PATRIC; fig|339670.21.peg.2359; -.
DR eggNOG; COG2003; Bacteria.
DR OMA; AMPDYEL; -.
DR Proteomes; UP000000662; Chromosome 1.
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; IPR001405; UPF0758.
DR InterPro; IPR020891; UPF0758_CS.
DR PANTHER; PTHR30471; PTHR30471; 1.
DR Pfam; PF04002; RadC; 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..258
FT /note="UPF0758 protein Bamb_2548"
FT /id="PRO_0000322670"
FT DOMAIN 136..258
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 207..220
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT COMPBIAS 28..42
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 258 AA; 28065 MW; 60275D2FAB39C1BA CRC64;
MLSPCLAAPA TECRDPADAP AAPARHTGPA RPRKRRPRNW KPHLPRERLL ERGPAALTDA
ELIALLLGTG GGGRDVFASA RALLARFGDS LRDMLDAEPD VFATHPGIGT ARSAVLIAVT
EIVRRALVEK ARERLQIDSP GAVEDYLRLR IGTRPHEVFV TLYLDARHGL IDVEESARGS
LTRMAVYPRE IVRRALVLNA AALIIAHNHP SGAVQPSAED RRLTRVLHEA LALIDAKLLD
HVVVGTADTF SFARAGWL
