Y1283_BRUSU
ID Y1283_BRUSU Reviewed; 249 AA.
AC P65956; G0KAP2; Q8YHS8;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=UPF0758 protein BR1283/BS1330_I1279;
GN Name=radC; OrderedLocusNames=BR1283, BS1330_I1279;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
CC -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}.
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DR EMBL; AE014291; AAN30201.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM18619.1; -; Genomic_DNA.
DR RefSeq; WP_002964401.1; NZ_KN046804.1.
DR AlphaFoldDB; P65956; -.
DR SMR; P65956; -.
DR EnsemblBacteria; AEM18619; AEM18619; BS1330_I1279.
DR GeneID; 45052312; -.
DR GeneID; 55590952; -.
DR KEGG; bms:BR1283; -.
DR KEGG; bsi:BS1330_I1279; -.
DR PATRIC; fig|204722.21.peg.3702; -.
DR HOGENOM; CLU_073529_0_0_5; -.
DR OMA; AMPDYEL; -.
DR PhylomeDB; P65956; -.
DR Proteomes; UP000007104; 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..249
FT /note="UPF0758 protein BR1283/BS1330_I1279"
FT /id="PRO_0000190689"
FT DOMAIN 127..249
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 198..211
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 249 AA; 27676 MW; 0DF77325A6F0638D CRC64;
MAKKKDTPGD GEFPGFSDTL QRTPKLEKPH YAGHRDRLKQ RFRDAPDALA DYELLELLLF
RAIRRADTKP IAKALLNRFG SIAEVLAAPE NLIAEIPGAG PTVALELKLV EAIAKRSARS
TVMEREVLGS WDKVINYCTA AMAFETREQF RILFLDKKNK LIADEVQQTG TVDHTPVYPR
EVVKRALELS ATAIILVHNH PSGDPTPSRA DIDMTKQLVN AAKALNITVH DHVIIGKHGH
ASLRSLRLI