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Chromosome partition protein MukB (Structural maintenance of chromosome-related protein)

 MUKB_ECOLI              Reviewed;        1486 AA.
P22523; P71227; P77164; Q47398;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
25-OCT-2017, entry version 170.
RecName: Full=Chromosome partition protein MukB;
AltName: Full=Structural maintenance of chromosome-related protein;
Name=mukB; OrderedLocusNames=b0924, JW0907;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=1989883;
Niki H., Jaffe A., Imamura R., Ogura T., Hiraga S.;
"The new gene mukB codes for a 177 kd protein with coiled-coil domains
involved in chromosome partitioning of E. coli.";
EMBO J. 10:183-193(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANTS MUKB33 AND MUKB106.
PubMed=7988894; DOI=10.1111/j.1574-6968.1994.tb07196.x;
Yamanaka K., Mitani T., Feng J., Ogura T., Niki H., Hiraga S.;
"Two mutant alleles of mukB, a gene essential for chromosome partition
in Escherichia coli.";
FEMS Microbiol. Lett. 123:27-31(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8905232; DOI=10.1093/dnares/3.3.137;
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=7513784;
Feng J., Yamanaka K., Niki H., Ogura T., Hiraga S.;
"New killing system controlled by two genes located immediately
upstream of the mukB gene in Escherichia coli.";
Mol. Gen. Genet. 243:136-147(1994).
[7]
PROTEIN SEQUENCE OF 9-21; 41-61; 353-363 AND 681-709, MODIFIES
FUNCTION OF TOPOISOMERASE IV, INTERACTION WITH MUKE; MUKF; ACP AND
PARC, AND MUTAGENESIS OF GLU-688 AND ASP-692.
PubMed=20921377; DOI=10.1073/pnas.1008678107;
Li Y., Stewart N.K., Berger A.J., Vos S., Schoeffler A.J.,
Berger J.M., Chait B.T., Oakley M.G.;
"Escherichia coli condensin MukB stimulates topoisomerase IV activity
by a direct physical interaction.";
Proc. Natl. Acad. Sci. U.S.A. 107:18832-18837(2010).
[8]
SUBUNIT.
PubMed=1464330;
Niki H., Imamura R., Kitaoka M., Yamanaka K., Ogura T., Hiraga S.;
"E.coli MukB protein involved in chromosome partition forms a
homodimer with a rod-and-hinge structure having DNA binding and
ATP/GTP binding activities.";
EMBO J. 11:5101-5109(1992).
[9]
INTERACTION WITH FTSZ.
PubMed=9688555; DOI=10.1016/S0014-5793(98)00677-2;
Lockhart A., Kendrick-Jones J.;
"Interaction of the N-terminal domain of MukB with the bacterial
tubulin homologue FtsZ.";
FEBS Lett. 430:278-282(1998).
[10]
INTERACTION WITH MUKE AND MUKF, AND MUTAGENESIS OF SER-33; LYS-40;
ASP-1201; VAL-1381; LEU-1403; PHE-1404; ASP-1406; MET-1428 AND
GLN-1429.
PubMed=10545099; DOI=10.1093/emboj/18.21.5873;
Yamazoe M., Onogi T., Sunako Y., Niki H., Yamanaka K., Ichimura T.,
Hiraga S.;
"Complex formation of MukB, MukE and MukF proteins involved in
chromosome partitioning in Escherichia coli.";
EMBO J. 18:5873-5884(1999).
[11]
FUNCTION.
PubMed=10660686; DOI=10.1073/pnas.030528397;
Sawitzke J.A., Austin S.;
"Suppression of chromosome segregation defects of Escherichia coli muk
mutants by mutations in topoisomerase I.";
Proc. Natl. Acad. Sci. U.S.A. 97:1671-1676(2000).
[12]
SUBCELLULAR LOCATION.
PubMed=11886550; DOI=10.1046/j.1365-2958.2001.02691.x;
den Blaauwen T., Lindqvist A., Loewe J., Nanninga N.;
"Distribution of the Escherichia coli structural maintenance of
chromosomes (SMC)-like protein MukB in the cell.";
Mol. Microbiol. 42:1179-1188(2001).
[13]
IDENTIFICATION IN A COMPLEX WITH SPOT; ISCS AND ACP.
PubMed=12885413; DOI=10.1016/S0014-5793(03)00746-4;
Gully D., Moinier D., Loiseau L., Bouveret E.;
"New partners of acyl carrier protein detected in Escherichia coli by
tandem affinity purification.";
FEBS Lett. 548:90-96(2003).
[14]
SUBCELLULAR LOCATION.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=22380631; DOI=10.1111/j.1365-2958.2012.08021.x;
Li G., Young K.D.;
"Isolation and identification of new inner membrane-associated
proteins that localize to cell poles in Escherichia coli.";
Mol. Microbiol. 84:276-295(2012).
[15]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-227.
PubMed=10545328; DOI=10.1016/S0969-2126(00)80052-0;
van den Ent F., Lockhart A., Kendrick-Jones J., Loewe J.;
"Crystal structure of the N-terminal domain of MukB: a protein
involved in chromosome partitioning.";
Structure 7:1181-1187(1999).
-!- FUNCTION: Plays a central role in chromosome condensation,
segregation and cell cycle progression. Functions as a homodimer,
which is essential for chromosome partition. Involved in negative
DNA supercoiling in vivo, and by this means organizes and compacts
chromosomes. May achieve or facilitate chromosome segregation by
condensation of DNA from both sides of a centrally located
replisome during cell division. Stimulates both DNA relaxation and
to a lesser extent decatenation activity of topoisomerase IV.
{ECO:0000269|PubMed:10660686}.
-!- SUBUNIT: Homodimerization via its hinge domain. Binds to DNA via
its C-terminal region. Interacts, and probably forms a ternary
complex, with MukE and MukF via its C-terminal region. The complex
formation is stimulated by calcium or magnesium. Interacts with
tubulin-related protein FtsZ. Identified in a complex with SpoT;
IscS and ACP. Interacts with the ParC subunit of topoisomerase IV.
{ECO:0000269|PubMed:10545099, ECO:0000269|PubMed:12885413,
ECO:0000269|PubMed:1464330, ECO:0000269|PubMed:20921377,
ECO:0000269|PubMed:9688555}.
-!- INTERACTION:
P0AFI2:parC; NbExp=11; IntAct=EBI-542943, EBI-878544;
-!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid
{ECO:0000269|PubMed:11886550, ECO:0000269|PubMed:22380631}.
Note=Restricted to the nucleoid region, far from the cell poles.
-!- DOMAIN: The hinge domain, which separates the large intramolecular
coiled coil regions, allows the homodimerization, forming a V-
shaped homodimer. The N- and C-terminus together form the head
domain.
-!- SIMILARITY: Belongs to the SMC family. MukB subfamily.
{ECO:0000305}.
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EMBL; X57550; CAA40776.1; -; Genomic_DNA.
EMBL; D31701; BAA06510.1; -; Genomic_DNA.
EMBL; U00096; AAC74010.1; -; Genomic_DNA.
EMBL; AP009048; BAA35670.1; -; Genomic_DNA.
EMBL; D26440; BAA05459.1; -; Genomic_DNA.
PIR; C64832; C64832.
PIR; JH0228; JH0228.
RefSeq; NP_415444.1; NC_000913.3.
RefSeq; WP_000572698.1; NZ_LN832404.1.
PDB; 1QHL; X-ray; 2.20 A; A=1-227.
PDB; 2WMM; X-ray; 2.30 A; A/B=645-804.
PDB; 3IBP; X-ray; 3.10 A; A=566-863.
PDB; 4MN4; X-ray; 2.30 A; C/D=645-804.
PDBsum; 1QHL; -.
PDBsum; 2WMM; -.
PDBsum; 3IBP; -.
PDBsum; 4MN4; -.
ProteinModelPortal; P22523; -.
SMR; P22523; -.
BioGrid; 4261687; 401.
DIP; DIP-10273N; -.
IntAct; P22523; 58.
MINT; MINT-1225884; -.
STRING; 316385.ECDH10B_0994; -.
PaxDb; P22523; -.
PRIDE; P22523; -.
EnsemblBacteria; AAC74010; AAC74010; b0924.
EnsemblBacteria; BAA35670; BAA35670; BAA35670.
GeneID; 945549; -.
KEGG; ecj:JW0907; -.
KEGG; eco:b0924; -.
PATRIC; fig|1411691.4.peg.1352; -.
EchoBASE; EB0613; -.
EcoGene; EG10618; mukB.
eggNOG; ENOG4105DUC; Bacteria.
eggNOG; COG3096; LUCA.
HOGENOM; HOG000278243; -.
InParanoid; P22523; -.
KO; K03632; -.
PhylomeDB; P22523; -.
BioCyc; EcoCyc:EG10618-MONOMER; -.
EvolutionaryTrace; P22523; -.
PRO; PR:P22523; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0000796; C:condensin complex; IDA:EcoCyc.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IDA:EcoCyc.
GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
GO; GO:0005525; F:GTP binding; IDA:EcoCyc.
GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
GO; GO:0051301; P:cell division; IMP:EcoCyc.
GO; GO:0030261; P:chromosome condensation; IDA:EcoCyc.
GO; GO:0007059; P:chromosome segregation; IMP:EcoliWiki.
GO; GO:0007062; P:sister chromatid cohesion; IMP:EcoliWiki.
HAMAP; MF_01800; MukB; 1.
InterPro; IPR012090; MukB.
InterPro; IPR032520; MukB_hinge.
InterPro; IPR007406; MukB_N_dom.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF04310; MukB; 1.
Pfam; PF16330; MukB_hinge; 1.
PIRSF; PIRSF005246; MukB; 1.
SUPFAM; SSF52540; SSF52540; 3.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell cycle; Cell division;
Chromosome partition; Coiled coil; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA condensation; DNA-binding;
Nucleotide-binding; Reference proteome.
CHAIN 1 1486 Chromosome partition protein MukB.
/FTId=PRO_0000068214.
NP_BIND 34 41 ATP. {ECO:0000255}.
REGION 645 804 Sufficient for ParC binding.
REGION 666 783 Flexible hinge.
COILED 326 418 {ECO:0000255}.
COILED 444 480 {ECO:0000255}.
COILED 509 603 {ECO:0000255}.
COILED 835 923 {ECO:0000255}.
COILED 977 1115 {ECO:0000255}.
COILED 1209 1266 {ECO:0000255}.
MUTAGEN 33 33 S->F: In mukB106; no effect.
{ECO:0000269|PubMed:10545099}.
MUTAGEN 40 40 K->L: No effect.
{ECO:0000269|PubMed:10545099}.
MUTAGEN 688 688 E->A: Does not rescue a ts-mutant of
MukB. {ECO:0000269|PubMed:20921377}.
MUTAGEN 692 692 D->A: Does not rescue a ts-mutant of
MukB; less binding of ParC.
{ECO:0000269|PubMed:20921377}.
MUTAGEN 1201 1201 D->N: In mukB33; no effect.
{ECO:0000269|PubMed:10545099}.
MUTAGEN 1381 1381 V->L: Abolishes DNA-binding, but remains
associated with MukE and MukF.
{ECO:0000269|PubMed:10545099}.
MUTAGEN 1403 1403 L->P: Abolishes association with MukE and
MukF, but still binds DNA.
{ECO:0000269|PubMed:10545099}.
MUTAGEN 1404 1404 F->L: No effect.
{ECO:0000269|PubMed:10545099}.
MUTAGEN 1406 1406 D->N: No effect.
{ECO:0000269|PubMed:10545099}.
MUTAGEN 1428 1428 M->L: No effect.
{ECO:0000269|PubMed:10545099}.
MUTAGEN 1429 1429 Q->R: Abolishes association with MukE and
MukF, but still binds DNA.
{ECO:0000269|PubMed:10545099}.
CONFLICT 266 266 A -> R (in Ref. 1; CAA40776 and 2;
BAA06510). {ECO:0000305}.
CONFLICT 318 319 EH -> DD (in Ref. 1; CAA40776).
{ECO:0000305}.
CONFLICT 1134 1134 H -> D (in Ref. 1; CAA40776).
{ECO:0000305}.
CONFLICT 1174 1175 SE -> VQ (in Ref. 1; CAA40776).
{ECO:0000305}.
CONFLICT 1276 1277 Missing (in Ref. 1; CAA40776 and 2;
BAA06510). {ECO:0000305}.
CONFLICT 1357 1380 WLRAESGALSTGEAIGTGMSILVM -> CCAQSLVHCRPVR
RWYRYVDSGV (in Ref. 1; CAA40776).
{ECO:0000305}.
CONFLICT 1390 1486 RRLRGKDISPCRLLFLDEAARLDARSIATLFELCERLQMQL
IIAAPENISPEKGTTYKLVRKVFQNTEHVHVVGLRGFAPQL
PETLPGTDEAPSQAS -> AACAVKISLLAACCSSMKQRDW
MLVLSPRCLNCVSVCKCNSSSQRRKISARRKAPPINWCVKS
SRIPNTFMSSACEDLRRNSLKRFQELTKRLLRRVKIKQQCR
LFFFRKLRFCTKKVAHYGALFFKLLYIRLCKNVRRLYTEDK
PDE (in Ref. 1; CAA40776). {ECO:0000305}.
STRAND 6 15 {ECO:0000244|PDB:1QHL}.
STRAND 18 23 {ECO:0000244|PDB:1QHL}.
HELIX 25 33 {ECO:0000244|PDB:1QHL}.
HELIX 38 51 {ECO:0000244|PDB:1QHL}.
TURN 55 57 {ECO:0000244|PDB:1QHL}.
HELIX 78 80 {ECO:0000244|PDB:1QHL}.
STRAND 83 93 {ECO:0000244|PDB:1QHL}.
STRAND 99 108 {ECO:0000244|PDB:1QHL}.
TURN 112 114 {ECO:0000244|PDB:1QHL}.
STRAND 116 125 {ECO:0000244|PDB:1QHL}.
HELIX 132 136 {ECO:0000244|PDB:1QHL}.
STRAND 141 143 {ECO:0000244|PDB:1QHL}.
HELIX 150 158 {ECO:0000244|PDB:1QHL}.
STRAND 164 167 {ECO:0000244|PDB:1QHL}.
HELIX 171 180 {ECO:0000244|PDB:1QHL}.
STRAND 183 186 {ECO:0000244|PDB:1QHL}.
HELIX 191 205 {ECO:0000244|PDB:1QHL}.
STRAND 206 208 {ECO:0000244|PDB:1QHL}.
HELIX 210 220 {ECO:0000244|PDB:1QHL}.
HELIX 573 617 {ECO:0000244|PDB:3IBP}.
HELIX 645 663 {ECO:0000244|PDB:2WMM}.
HELIX 674 681 {ECO:0000244|PDB:2WMM}.
HELIX 686 689 {ECO:0000244|PDB:2WMM}.
HELIX 690 692 {ECO:0000244|PDB:2WMM}.
TURN 695 697 {ECO:0000244|PDB:2WMM}.
HELIX 698 704 {ECO:0000244|PDB:2WMM}.
HELIX 706 710 {ECO:0000244|PDB:2WMM}.
STRAND 712 715 {ECO:0000244|PDB:2WMM}.
HELIX 717 719 {ECO:0000244|PDB:2WMM}.
HELIX 721 724 {ECO:0000244|PDB:2WMM}.
STRAND 732 739 {ECO:0000244|PDB:2WMM}.
STRAND 743 745 {ECO:0000244|PDB:4MN4}.
STRAND 751 754 {ECO:0000244|PDB:2WMM}.
STRAND 757 763 {ECO:0000244|PDB:2WMM}.
STRAND 766 771 {ECO:0000244|PDB:2WMM}.
HELIX 780 802 {ECO:0000244|PDB:2WMM}.
TURN 825 828 {ECO:0000244|PDB:3IBP}.
STRAND 829 831 {ECO:0000244|PDB:3IBP}.
HELIX 834 853 {ECO:0000244|PDB:3IBP}.
SEQUENCE 1486 AA; 170230 MW; 38C7874BEB78D6D6 CRC64;
MIERGKFRSL TLINWNGFFA RTFDLDELVT TLSGGNGAGK STTMAAFVTA LIPDLTLLHF
RNTTEAGATS GSRDKGLHGK LKAGVCYSML DTINSRHQRV VVGVRLQQVA GRDRKVDIKP
FAIQGLPMSV QPTQLVTETL NERQARVLPL NELKDKLEAM EGVQFKQFNS ITDYHSLMFD
LGIIARRLRS ASDRSKFYRL IEASLYGGIS SAITRSLRDY LLPENSGVRK AFQDMEAALR
ENRMTLEAIR VTQSDRDLFK HLISEATNYV AADYMRHANE RRVHLDKALE FRRELHTSRQ
QLAAEQYKHV DMARELAEHN GAEGDLEADY QAASDHLNLV QTALRQQEKI ERYEADLDEL
QIRLEEQNEV VAEAIERQQE NEARAEAAEL EVDELKSQLA DYQQALDVQQ TRAIQYNQAI
AALNRAKELC HLPDLTADCA AEWLETFQAK ELEATEKMLS LEQKMSMAQT AHSQFEQAYQ
LVVAINGPLA RNEAWDVARE LLREGVDQRH LAEQVQPLRM RLSELEQRLR EQQEAERLLA
DFCKRQGKNF DIDELEALHQ ELEARIASLS DSVSNAREER MALRQEQEQL QSRIQSLMQR
APVWLAAQNS LNQLSEQCGE EFTSSQDVTE YLQQLLERER EAIVERDEVG ARKNAVDEEI
ERLSQPGGSE DQRLNALAER FGGVLLSEIY DDVSLEDAPY FSALYGPSRH AIVVPDLSQV
TEHLEGLTDC PEDLYLIEGD PQSFDDSVFS VDELEKAVVV KIADRQWRYS RFPEVPLFGR
AARESRIESL HAEREVLSER FATLSFDVQK TQRLHQAFSR FIGSHLAVAF ESDPEAEIRQ
LNSRRVELER ALSNHENDNQ QQRIQFEQAK EGVTALNRIL PRLNLLADDS LADRVDEIRE
RLDEAQEAAR FVQQFGNQLA KLEPIVSVLQ SDPEQFEQLK EDYAYSQQMQ RDARQQAFAL
TEVVQRRAHF SYSDSAEMLS GNSDLNEKLR ERLEQAEAER TRAREALRGH AAQLSQYNQV
LASLKSSYDT KKELLNDLQR ELQDIGVRAD SGAEERARIR RDELHAQLSN NRSRRNQLEK
ALTFCEAEMD NLTRKLRKLE RDYFEMREQV VTAKAGWCAV MRMVKDNGVE RRLHRRELAY
LSADDLRSMS DKALGALRLA VADNEHLRDV LRMSEDPKRP ERKIQFFVAV YQHLRERIRQ
DIIRTDDPVE AIEQMEIELS RLTEELTSRE QKLAISSRSV ANIIRKTIQR EQNRIRMLNQ
GLQNVSFGQV NSVRLNVNVR ETHAMLLDVL SEQHEQHQDL FNSNRLTFSE ALAKLYQRLN
PQIDMGQRTP QTIGEELLDY RNYLEMEVEV NRGSDGWLRA ESGALSTGEA IGTGMSILVM
VVQSWEDESR RLRGKDISPC RLLFLDEAAR LDARSIATLF ELCERLQMQL IIAAPENISP
EKGTTYKLVR KVFQNTEHVH VVGLRGFAPQ LPETLPGTDE APSQAS


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28-542 The protein encoded by MCM4 is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein comp 0.1 mg
28-540 MCM7 encodes a protein that is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein comp 0.1 mg
28-539 MCM7 encodes a protein that is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein comp 0.1 mg
28-535 The protein encoded by MCM2 is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are involved in the initiation of eukaryotic genome replication. The hexameric protein comple 0.1 mg


 

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