Y2230_BURMA
ID Y2230_BURMA Reviewed; 278 AA.
AC Q62HM6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=UPF0758 protein BMA2230;
GN OrderedLocusNames=BMA2230;
OS Burkholderia mallei (strain ATCC 23344).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=243160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23344;
RX PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT "Structural flexibility in the Burkholderia mallei genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
CC -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}.
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DR EMBL; CP000010; AAU50257.1; -; Genomic_DNA.
DR RefSeq; WP_004185928.1; NC_006348.1.
DR RefSeq; YP_103794.1; NC_006348.1.
DR AlphaFoldDB; Q62HM6; -.
DR SMR; Q62HM6; -.
DR STRING; 243160.BMA2230; -.
DR EnsemblBacteria; AAU50257; AAU50257; BMA2230.
DR GeneID; 56594773; -.
DR KEGG; bma:BMA2230; -.
DR PATRIC; fig|243160.12.peg.2294; -.
DR eggNOG; COG2003; Bacteria.
DR HOGENOM; CLU_073529_0_1_4; -.
DR OMA; AMPDYEL; -.
DR Proteomes; UP000006693; 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; 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 BMA2230"
FT /id="PRO_0000322671"
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
