MFPA_MYCTU
ID MFPA_MYCTU Reviewed; 183 AA.
AC I6YBX3;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Pentapeptide repeat protein MfpA {ECO:0000303|PubMed:15933203};
DE Short=MfpAMt {ECO:0000303|PubMed:19060136};
GN Name=mfpA {ECO:0000303|PubMed:15933203}; OrderedLocusNames=Rv3361c;
GN ORFNames=LH57_18360;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RA Hazbon M.H., Riojas M.A., Damon A.M., Alalade R.O., Cantwell B.J.,
RA Monaco A., King S., Sohrabi A.;
RT "Phylogenetic analysis of Mycobacterial species using whole genome
RT sequences.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBUNIT, DOMAIN, AND FOLDING KINETICS.
RC STRAIN=H37Rv;
RX PubMed=18977756; DOI=10.1074/jbc.m804702200;
RA Khrapunov S., Cheng H., Hegde S., Blanchard J., Brenowitz M.;
RT "Solution structure and refolding of the Mycobacterium tuberculosis
RT pentapeptide repeat protein MfpA.";
RL J. Biol. Chem. 283:36290-36299(2008).
RN [4]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=H37Rv;
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).
RN [5]
RP FOLDING KINETICS.
RC STRAIN=H37Rv;
RX PubMed=21605934; DOI=10.1016/j.bpc.2011.04.015;
RA Khrapunov S., Brenowitz M.;
RT "Stability, denaturation and refolding of Mycobacterium tuberculosis MfpA,
RT a DNA mimicking protein that confers antibiotic resistance.";
RL Biophys. Chem. 159:33-40(2011).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), FUNCTION IN E.COLI, SUBUNIT, AND
RP DOMAIN.
RC STRAIN=H37Rv;
RX PubMed=15933203; DOI=10.1126/science.1110699;
RA Hegde S.S., Vetting M.W., Roderick S.L., Mitchenall L.A., Maxwell A.,
RA Takiff H.E., Blanchard J.S.;
RT "A fluoroquinolone resistance protein from Mycobacterium tuberculosis that
RT mimics DNA.";
RL Science 308:1480-1483(2005).
CC -!- FUNCTION: Might be involved in fluoroquinolone resistance
CC (PubMed:15933203). Inhibits ATP-independent DNA relaxation, ATP-
CC dependent DNA supercoiling and ATP-dependent decatenation by endogenous
CC gyrase, 50% inhibition occurs at 2 uM; inhibition is abolished if GyrA
CC is mutated (Asp-87 to Gly or His) (PubMed:19060136). Also inhibits
CC fluoroquinolone-promoted dsDNA cleavage (PubMed:19060136). Increases
CC fluoroquinolone (ciprofloxacin or moxifloxacin) inhibition of gyrase
CC supercoiling activity in a concentration-dependent manner
CC (PubMed:19060136). Inhibits DNA relaxation and supercoiling by E.coli
CC gyrase (PubMed:15933203). Forms a structure that exhibits size, shape
CC and electrostatic similarity to B-form DNA; it may bind to DNA gyrase
CC which is postulated to protect it from fluoroquinolones
CC (PubMed:15933203). {ECO:0000269|PubMed:15933203,
CC ECO:0000269|PubMed:19060136}.
CC -!- SUBUNIT: Homodimer. Probably interacts with DNA gyrase.
CC {ECO:0000269|PubMed:18977756, ECO:0000305|PubMed:15933203,
CC ECO:0000305|PubMed:19060136}.
CC -!- DOMAIN: Each subunit forms a right-handed beta-helix with 8 complete
CC coils that stack upon each other. {ECO:0000269|PubMed:15933203,
CC ECO:0000269|PubMed:18977756}.
CC -!- SIMILARITY: Belongs to the pentapeptide repeat protein family.
CC {ECO:0000305}.
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DR EMBL; CP009480; AIR16154.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP46182.1; -; Genomic_DNA.
DR RefSeq; NP_217878.1; NC_000962.3.
DR RefSeq; WP_003417767.1; NZ_NVQJ01000052.1.
DR PDB; 2BM4; X-ray; 2.20 A; A/B=1-183.
DR PDB; 2BM5; X-ray; 2.00 A; A/B=1-183.
DR PDB; 2BM6; X-ray; 2.20 A; A=1-183.
DR PDB; 2BM7; X-ray; 2.70 A; A/B/C=1-183.
DR PDBsum; 2BM4; -.
DR PDBsum; 2BM5; -.
DR PDBsum; 2BM6; -.
DR PDBsum; 2BM7; -.
DR AlphaFoldDB; I6YBX3; -.
DR SMR; I6YBX3; -.
DR STRING; 83332.Rv3361c; -.
DR PaxDb; I6YBX3; -.
DR PRIDE; I6YBX3; -.
DR DNASU; 888130; -.
DR GeneID; 45427360; -.
DR GeneID; 888130; -.
DR KEGG; mtu:Rv3361c; -.
DR PATRIC; fig|83332.111.peg.3750; -.
DR TubercuList; Rv3361c; -.
DR eggNOG; COG1357; Bacteria.
DR HOGENOM; CLU_033401_5_5_11; -.
DR OMA; ADFFDCK; -.
DR PhylomeDB; I6YBX3; -.
DR Proteomes; UP000001584; Chromosome.
DR InterPro; IPR001646; 5peptide_repeat.
DR Pfam; PF00805; Pentapeptide; 1.
DR Pfam; PF13599; Pentapeptide_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome.
FT CHAIN 1..183
FT /note="Pentapeptide repeat protein MfpA"
FT /id="PRO_0000434153"
FT DOMAIN 113..147
FT /note="Pentapeptide repeat"
FT /evidence="ECO:0000255"
SQ SEQUENCE 183 AA; 20020 MW; D4830FF752235A69 CRC64;
MQQWVDCEFT GRDFRDEDLS RLHTERAMFS ECDFSGVNLA ESQHRGSAFR NCTFERTTLW
HSTFAQCSML GSVFVACRLR PLTLDDVDFT LAVLGGNDLR GLNLTGCRLR ETSLVDTDLR
KCVLRGADLS GARTTGARLD DADLRGATVD PVLWRTASLV GARVDVDQAV AFAAAHGLCL
AGG
