Y1789_COXBN
ID Y1789_COXBN Reviewed; 224 AA.
AC A9KGS6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=UPF0758 protein CBUD_1789;
GN OrderedLocusNames=CBUD_1789;
OS Coxiella burnetii (strain Dugway 5J108-111).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=434922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dugway 5J108-111;
RX PubMed=19047403; DOI=10.1128/iai.01141-08;
RA Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E.,
RA Heinzen R.A.;
RT "Comparative genomics reveal extensive transposon-mediated genomic
RT plasticity and diversity among potential effector proteins within the genus
RT Coxiella.";
RL Infect. Immun. 77:642-656(2009).
CC -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000733; ABS77915.1; -; Genomic_DNA.
DR RefSeq; WP_005771440.1; NC_009727.1.
DR AlphaFoldDB; A9KGS6; -.
DR SMR; A9KGS6; -.
DR EnsemblBacteria; ABS77915; ABS77915; CBUD_1789.
DR KEGG; cbd:CBUD_1789; -.
DR HOGENOM; CLU_073529_0_2_6; -.
DR OMA; AMPDYEL; -.
DR OrthoDB; 1833204at2; -.
DR Proteomes; UP000008555; Chromosome.
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..224
FT /note="UPF0758 protein CBUD_1789"
FT /id="PRO_1000074143"
FT DOMAIN 102..224
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOTIF 173..186
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 224 AA; 25193 MW; DB2F2E4FB3B271A5 CRC64;
MSITQWPTSE RPREKLLRED AHILSDAELI AVIIQKGVRG CNAVELAREW LNHLGGLASL
LNADFHRLSG LRGLGKAVYC KLKAAAELQR RYLRQSLERK GQLGCTQDAQ QLLYAQLRHH
ESEVFACLFL DNRHRIIQFE KLFYGSINQA SVHPREIIKR ALYHNSAALI VAHNHPSGVP
DPSQADRAAT THLKEALALI DVRLLDHIII GDRNSFSFAE SGLL