MUKF_ECOLI
ID MUKF_ECOLI Reviewed; 440 AA.
AC P60293; P36567;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Chromosome partition protein MukF;
DE AltName: Full=Protein KicB;
GN Name=mukF; Synonyms=kicB; OrderedLocusNames=b0922, JW0905;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7513784; DOI=10.1007/bf00280310;
RA Feng J., Yamanaka K., Niki H., Ogura T., Hiraga S.;
RT "New killing system controlled by two genes located immediately upstream of
RT the mukB gene in Escherichia coli.";
RL Mol. Gen. Genet. 243:136-147(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 162-176 AND 263-279, AND INTERACTION WITH MUKB.
RX PubMed=20921377; DOI=10.1073/pnas.1008678107;
RA Li Y., Stewart N.K., Berger A.J., Vos S., Schoeffler A.J., Berger J.M.,
RA Chait B.T., Oakley M.G.;
RT "Escherichia coli condensin MukB stimulates topoisomerase IV activity by a
RT direct physical interaction.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:18832-18837(2010).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF LEU-233.
RX PubMed=8602138; DOI=10.1007/bf02174381;
RA Yamanaka K., Ogura T., Niki H., Hiraga S.;
RT "Identification of two new genes, mukE and mukF, involved in chromosome
RT partitioning in Escherichia coli.";
RL Mol. Gen. Genet. 250:241-251(1996).
RN [7]
RP CHARACTERIZATION, AND INTERACTION WITH MUKB AND MUKE.
RX PubMed=10545099; DOI=10.1093/emboj/18.21.5873;
RA Yamazoe M., Onogi T., Sunako Y., Niki H., Yamanaka K., Ichimura T.,
RA Hiraga S.;
RT "Complex formation of MukB, MukE and MukF proteins involved in chromosome
RT partitioning in Escherichia coli.";
RL EMBO J. 18:5873-5884(1999).
CC -!- FUNCTION: Involved in chromosome condensation, segregation and cell
CC cycle progression. May participate in facilitating chromosome
CC segregation by condensation DNA from both sides of a centrally located
CC replisome during cell division. Not required for mini-F plasmid
CC partitioning. Probably acts via its interaction with MukB and MukE.
CC Overexpression results in anucleate cells. It has a calcium binding
CC activity. {ECO:0000269|PubMed:8602138}.
CC -!- SUBUNIT: Interacts, and probably forms a ternary complex, with MukE and
CC MukB via its C-terminal region. The complex formation is stimulated by
CC calcium or magnesium. It is required for an interaction between MukE
CC and MukB. {ECO:0000269|PubMed:10545099, ECO:0000269|PubMed:20921377}.
CC -!- INTERACTION:
CC P60293; P22524: mukE; NbExp=6; IntAct=EBI-554679, EBI-554672;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid. Note=Restricted to the
CC nucleoid region.
CC -!- SIMILARITY: Belongs to the MukF family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a killing factor. PubMed:8602138
CC showed that it is not involved in killing system. {ECO:0000305}.
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DR EMBL; D26440; BAA05457.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74008.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35668.1; -; Genomic_DNA.
DR PIR; S43911; S43911.
DR RefSeq; NP_415442.1; NC_000913.3.
DR RefSeq; WP_001288850.1; NZ_STEB01000006.1.
DR PDB; 1T98; X-ray; 2.90 A; A/B=1-287.
DR PDB; 3EUH; X-ray; 2.90 A; A/B=1-440.
DR PDB; 3RPU; X-ray; 3.60 A; A/B/X=1-440.
DR PDBsum; 1T98; -.
DR PDBsum; 3EUH; -.
DR PDBsum; 3RPU; -.
DR AlphaFoldDB; P60293; -.
DR SMR; P60293; -.
DR BioGRID; 4260007; 248.
DR ComplexPortal; CPX-1090; MukBEF condensin complex.
DR DIP; DIP-39981N; -.
DR IntAct; P60293; 3.
DR MINT; P60293; -.
DR STRING; 511145.b0922; -.
DR jPOST; P60293; -.
DR PaxDb; P60293; -.
DR PRIDE; P60293; -.
DR EnsemblBacteria; AAC74008; AAC74008; b0922.
DR EnsemblBacteria; BAA35668; BAA35668; BAA35668.
DR GeneID; 66670802; -.
DR GeneID; 945548; -.
DR KEGG; ecj:JW0905; -.
DR KEGG; eco:b0922; -.
DR PATRIC; fig|1411691.4.peg.1354; -.
DR EchoBASE; EB2084; -.
DR eggNOG; COG3006; Bacteria.
DR HOGENOM; CLU_049853_0_0_6; -.
DR OMA; AIYNNER; -.
DR PhylomeDB; P60293; -.
DR BioCyc; EcoCyc:EG12165-MON; -.
DR EvolutionaryTrace; P60293; -.
DR PRO; PR:P60293; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0000796; C:condensin complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030261; P:chromosome condensation; IC:ComplexPortal.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd16337; MukF_C; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.225.40; -; 1.
DR Gene3D; 1.20.58.590; -; 1.
DR HAMAP; MF_01803; MukF; 1.
DR InterPro; IPR005582; Chromosome_partition_MukF.
DR InterPro; IPR033441; MukF_C.
DR InterPro; IPR038198; MukF_C_sf.
DR InterPro; IPR033440; MukF_M.
DR InterPro; IPR036141; MukF_M_sp.
DR InterPro; IPR033439; MukF_WHTH.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF03882; KicB; 1.
DR Pfam; PF17193; MukF_C; 1.
DR Pfam; PF17192; MukF_M; 1.
DR PIRSF; PIRSF018282; MukF; 1.
DR SUPFAM; SSF140570; SSF140570; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell cycle; Cell division; Chromosome partition;
KW Cytoplasm; Direct protein sequencing; DNA condensation; Reference proteome.
FT CHAIN 1..440
FT /note="Chromosome partition protein MukF"
FT /id="PRO_0000211600"
FT REGION 208..236
FT /note="Leucine-zipper"
FT MUTAGEN 233
FT /note="L->P: Abolishes function."
FT /evidence="ECO:0000269|PubMed:8602138"
FT HELIX 10..18
FT /evidence="ECO:0007829|PDB:1T98"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:1T98"
FT HELIX 26..40
FT /evidence="ECO:0007829|PDB:1T98"
FT HELIX 49..62
FT /evidence="ECO:0007829|PDB:1T98"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:1T98"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:1T98"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1T98"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:1T98"
FT HELIX 122..144
FT /evidence="ECO:0007829|PDB:1T98"
FT HELIX 149..155
FT /evidence="ECO:0007829|PDB:1T98"
FT HELIX 157..162
FT /evidence="ECO:0007829|PDB:1T98"
FT HELIX 164..195
FT /evidence="ECO:0007829|PDB:1T98"
FT HELIX 197..241
FT /evidence="ECO:0007829|PDB:1T98"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:1T98"
FT HELIX 247..279
FT /evidence="ECO:0007829|PDB:1T98"
FT TURN 288..291
FT /evidence="ECO:0007829|PDB:3EUH"
FT HELIX 297..306
FT /evidence="ECO:0007829|PDB:3EUH"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:3EUH"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:3EUH"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:3EUH"
SQ SEQUENCE 440 AA; 50579 MW; 55824FD545247EE8 CRC64;
MSEFSQTVPE LVAWARKNDF SISLPVDRLS FLLAVATLNG ERLDGEMSEG ELVDAFRHVS
DAFEQTSETI GVRANNAIND MVRQRLLNRF TSEQAEGNAI YRLTPLGIGI TDYYIRQREF
STLRLSMQLS IVAGELKRAA DAAEEGGDEF HWHRNVYAPL KYSVAEIFDS IDLTQRLMDE
QQQQVKDDIA QLLNKDWRAA ISSCELLLSE TSGTLRELQD TLEAAGDKLQ ANLLRIQDAT
MTHDDLHFVD RLVFDLQSKL DRIISWGQQS IDLWIGYDRH VHKFIRTAID MDKNRVFAQR
LRQSVQTYFD EPWALTYANA DRLLDMRDEE MALRDEEVTG ELPEDLEYEE FNEIREQLAA
IIEEQLAVYK TRQVPLDLGL VVREYLSQYP RARHFDVARI VIDQAVRLGV AQADFTGLPA
KWQPINDYGA KVQAHVIDKY
