TUBR_PRIM1
ID TUBR_PRIM1 Reviewed; 101 AA.
AC Q848W2;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=DNA-binding protein TubR {ECO:0000303|PubMed:23010931};
GN Name=tubR {ECO:0000303|PubMed:23010931}; OrderedLocusNames=BMQ_pBM40059;
OS Priestia megaterium (strain ATCC 12872 / QMB1551) (Bacillus megaterium).
OG Plasmid pBM400.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=545693;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12872 / QMB1551; PLASMID=pBM400;
RX PubMed=14602653; DOI=10.1128/aem.69.11.6888-6898.2003;
RA Scholle M.D., White C.A., Kunnimalaiyaan M., Vary P.S.;
RT "Sequencing and characterization of pBM400 from Bacillus megaterium QM
RT B1551.";
RL Appl. Environ. Microbiol. 69:6888-6898(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12872 / QMB1551; PLASMID=pBM400;
RX PubMed=21705586; DOI=10.1128/jb.00449-11;
RA Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA Koenig S.S., Creasy H.H., Rosovitz M.J., Riley D.R., Daugherty S.,
RA Martin M., Elbourne L.D., Paulsen I., Biedendieck R., Braun C.,
RA Grayburn S., Dhingra S., Lukyanchuk V., Ball B., Ul-Qamar R., Seibel J.,
RA Bremer E., Jahn D., Ravel J., Vary P.S.;
RT "Genome sequences of the biotechnologically important Bacillus megaterium
RT strains QM B1551 and DSM319.";
RL J. Bacteriol. 193:4199-4213(2011).
RN [3] {ECO:0007744|PDB:4ASN}
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS), FUNCTION, SUBUNIT, AND DNA-BINDING.
RC STRAIN=ATCC 12872 / QMB1551; PLASMID=pBM400;
RX PubMed=23010931; DOI=10.1073/pnas.1210899109;
RA Aylett C.H., Lowe J.;
RT "Superstructure of the centromeric complex of TubZRC plasmid partitioning
RT systems.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:16522-16527(2012).
CC -!- FUNCTION: A DNA-binding protein that is part of the type III plasmid
CC partition system used to ensure correct segregation of the pBM400
CC plasmid. Binds the plasmid origin of replication, probably
CC cooperatively, forming a ring or short helix with external DNA
CC (PubMed:23010931). Its effect on RNA expression has not been shown
CC (Probable). {ECO:0000269|PubMed:23010931, ECO:0000305}.
CC -!- SUBUNIT: Homodimer. Dimers bind to DNA, forming a protein-bound
CC filament which may form a helix around the TubZ filament.
CC {ECO:0000269|PubMed:23010931}.
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DR EMBL; CP001987; AAO52804.1; -; Genomic_DNA.
DR RefSeq; WP_011106199.1; NC_004604.2.
DR PDB; 4ASN; X-ray; 3.50 A; A/B/C=1-101.
DR PDBsum; 4ASN; -.
DR AlphaFoldDB; Q848W2; -.
DR SMR; Q848W2; -.
DR EnsemblBacteria; AAO52804; AAO52804; BMQ_pBM40059.
DR KEGG; bmq:BMQ_pBM40059; -.
DR HOGENOM; CLU_2380079_0_0_9; -.
DR OrthoDB; 2176518at2; -.
DR Proteomes; UP000000935; Plasmid pBM400.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030541; P:plasmid partitioning; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Plasmid; Plasmid partition; Reference proteome.
FT CHAIN 1..101
FT /note="DNA-binding protein TubR"
FT /id="PRO_0000448566"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:4ASN"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:4ASN"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:4ASN"
FT HELIX 37..41
FT /evidence="ECO:0007829|PDB:4ASN"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:4ASN"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:4ASN"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:4ASN"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:4ASN"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:4ASN"
SQ SEQUENCE 101 AA; 11593 MW; FB2A79588FE55417 CRC64;
MSDYFEEVMR KLTIEDVSIL GWLFQNEANA VFKAIKKSSI ADELEYSTAN FRKTLNKLEA
IHFIGTVTGG KEHKLYLTEY GQQAVQQAIH HGEENEEVEE I