QNRB4_ECOLX
ID QNRB4_ECOLX Reviewed; 215 AA.
AC Q2PT27;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=Pentapeptide repeat protein QnrB4 {ECO:0000303|PubMed:21781207};
DE AltName: Full=Plasmid-mediated quinolone resistance determinant {ECO:0000303|PubMed:21781207};
GN Name=qnrB4 {ECO:0000303|PubMed:16870791};
OS Escherichia coli.
OG Plasmid pDEC216, and Plasmid pEC37Tc.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=16870791; DOI=10.1128/aac.01647-05;
RA Robicsek A., Strahilevitz J., Sahm D.F., Jacoby G.A., Hooper D.C.;
RT "qnr prevalence in ceftazidime-resistant Enterobacteriaceae isolates from
RT the United States.";
RL Antimicrob. Agents Chemother. 50:2872-2874(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=37Tc; PLASMID=pEC37Tc;
RX PubMed=21781207; DOI=10.1111/j.1469-0691.2011.03539.x;
RA Mata C., Miro E., Toleman M., Rivera M.A., Walsh T.R., Navarro F.;
RT "Association of bla(DHA-1) and qnrB genes carried by broad-host-range
RT plasmids among isolates of Enterobacteriaceae at a Spanish hospital.";
RL Clin. Microbiol. Infect. 17:1514-1517(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DEC216; PLASMID=pDEC216;
RA Hu G., Han Z.;
RT "Genetic environment of DHA-1 in Escherichia coli.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
RX PubMed=19060136; DOI=10.1128/jb.01205-08;
RA Merens A., Matrat S., Aubry A., Lascols C., Jarlier V., Soussy C.J.,
RA Cavallo J.D., Cambau E.;
RT "The pentapeptide repeat proteins MfpAMt and QnrB4 exhibit opposite effects
RT on DNA gyrase catalytic reactions and on the ternary gyrase-DNA-quinolone
RT complex.";
RL J. Bacteriol. 191:1587-1594(2009).
CC -!- FUNCTION: Probably plays a role in resistance to quinolone antibiotics
CC (PubMed:16870791). Only inhibits ATP-dependent DNA supercoiling by
CC E.coli gyrase at high concentration (30 uM) (PubMed:19060136). Protects
CC E.coli gyrase supercoiling activity from inhibition by fluoroquinolones
CC (ciprofloxacin) at 0.1 uM, does not protect M.tuberculosis gyrase
CC activity (PubMed:19060136). {ECO:0000269|PubMed:19060136,
CC ECO:0000305|PubMed:16870791}.
CC -!- MISCELLANEOUS: The gene for this protein has been isolated from
CC plasmids in multiple Enterobacteriaceae (PubMed:16870791,
CC PubMed:19060136). For experiments in situ it was cloned from E.cloacae
CC strain HM05-184 but tested in E.coli (PubMed:19060136).
CC {ECO:0000305|PubMed:16870791, ECO:0000305|PubMed:19060136}.
CC -!- SIMILARITY: Belongs to the pentapeptide repeat protein family.
CC {ECO:0000305}.
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DR EMBL; DQ303921; ABC17630.2; -; Genomic_DNA.
DR EMBL; HQ700359; AEJ36325.1; -; Genomic_DNA.
DR EMBL; KC848778; AGI55898.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2PT27; -.
DR SMR; Q2PT27; -.
DR PRIDE; Q2PT27; -.
DR KEGG; ag:ABC17630; -.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR InterPro; IPR001646; 5peptide_repeat.
DR Pfam; PF13599; Pentapeptide_4; 2.
PE 3: Inferred from homology;
KW Antibiotic resistance; Plasmid.
FT CHAIN 1..215
FT /note="Pentapeptide repeat protein QnrB4"
FT /id="PRO_0000434156"
FT DOMAIN 113..147
FT /note="Pentapeptide repeat"
FT /evidence="ECO:0000255"
SQ SEQUENCE 215 AA; 23979 MW; B7E0163A0D04217A CRC64;
MMTLALVGEK IDRNRFTGEK VENSTFFNCD FSGADLSGTE FIGCQFYDRE SQKGCNFSRA
NLKDAIFKSC DLSMADFRNI NALGIEIRHC RAQGSDFRGA SFMNMITTRT WFCSAYITNT
NLSYANFSKV VLEKCELWEN RWMGTQVLGA TFSGSDLSGG EFSSFDWRAA NVTHCDLTNS
ELGDLDIRGV DLQGVKLDSY QASLLLERLG IAVMG