P22523 (MUKB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chromosome partition protein MukB

Alternative name(s):
Structural maintenance of chromosome-related protein

Gene names

Name:	mukB
Ordered Locus Names:	b0924, JW0907

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	1486 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.7 Ref.11
Subunit structure	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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.13
Subcellular location	Cytoplasm › nucleoid. Note: Restricted to the nucleoid region, far from the cell poles. Ref.12 Ref.14
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. HAMAP-Rule MF_01800
Sequence similarities	Belongs to the SMC family. MukB subfamily.

Ontologies

Keywords
Biological process	Cell cycle Cell division Chromosome partition DNA condensation
Cellular component	Cytoplasm
Domain	Coiled coil
Ligand	ATP-binding DNA-binding Nucleotide-binding
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: HAMAP cell division Inferred from mutant phenotype Ref.1. Source: EcoCyc chromosome condensation Inferred from direct assay PubMed 18376412. Source: EcoCyc sister chromatid cohesion Inferred from mutant phenotype PubMed 14517265. Source: EcoliWiki
Cellular_component	condensin complex Inferred from direct assay PubMed 16740950. Source: EcoCyc cytoplasm Inferred from electronic annotation. Source: HAMAP nucleoid Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from direct assay Ref.8. Source: EcoCyc DNA binding Inferred from direct assay Ref.8. Source: EcoCyc GTP binding Inferred from direct assay Ref.8. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
parC	P0AFI2	3	EBI-542943,EBI-878544

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1486

1486

Chromosome partition protein MukB HAMAP-Rule MF_01800

PRO_0000068214

Regions

Nucleotide binding

34 – 41

8

ATP Potential

Region

645 – 804

160

Sufficient for ParC binding HAMAP-Rule MF_01800

Region

666 – 783

118

Flexible hinge HAMAP-Rule MF_01800

Coiled coil

326 – 418

93

Potential

Coiled coil

444 – 480

37

Potential

Coiled coil

509 – 603

95

Potential

Coiled coil

835 – 923

89

Potential

Coiled coil

977 – 1115

139

Potential

Coiled coil

1209 – 1266

58

Potential

Experimental info

Mutagenesis

33

1

S → F in mukB106; no effect. Ref.10

Mutagenesis

40

1

K → L: No effect. Ref.10

Mutagenesis

688

1

E → A: Does not rescue a ts-mutant of MukB. Ref.7

Mutagenesis

692

1

D → A: Does not rescue a ts-mutant of MukB; less binding of ParC. Ref.7

Mutagenesis

1201

1

D → N in mukB33; no effect. Ref.10

Mutagenesis

1381

1

V → L: Abolishes DNA-binding, but remains associated with MukE and MukF. Ref.10

Mutagenesis

1403

1

L → P: Abolishes association with MukE and MukF, but still binds DNA. Ref.10

Mutagenesis

1404

1

F → L: No effect. Ref.10

Mutagenesis

1406

1

D → N: No effect. Ref.10

Mutagenesis

1428

1

M → L: No effect. Ref.10

Mutagenesis

1429

1

Q → R: Abolishes association with MukE and MukF, but still binds DNA. Ref.10

Sequence conflict

266

1

A → R in CAA40776. Ref.1

Sequence conflict

266

1

A → R in BAA06510. Ref.2

Sequence conflict

318 – 319

2

EH → DD in CAA40776. Ref.1

Sequence conflict

1134

1

H → D in CAA40776. Ref.1

Sequence conflict

1174 – 1175

2

SE → VQ in CAA40776. Ref.1

Sequence conflict

1276 – 1277

2

Missing in CAA40776. Ref.1

Sequence conflict

1276 – 1277

2

Missing in BAA06510. Ref.2

Sequence conflict

1357 – 1380

24

WLRAE…SILVM → CCAQSLVHCRPVRRWYRYVD SGV in CAA40776. Ref.1

Sequence conflict

1390 – 1486

97

RRLRG…PSQAS → AACAVKISLLAACCSSMKQR DWMLVLSPRCLNCVSVCKCN SSSQRRKISARRKAPPINWC VKSSRIPNTFMSSACEDLRR NSLKRFQELTKRLLRRVKIK QQCRLFFFRKLRFCTKKVAH YGALFFKLLYIRLCKNVRRL YTEDKPDE in CAA40776. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1486

Helix Strand Turn

Details...

Beta strand

6 – 15

10

Beta strand

18 – 23

6

Helix

25 – 33

9

Helix

38 – 51

14

Turn

55 – 57

3

Helix

78 – 80

3

Beta strand

83 – 93

11

Beta strand

99 – 108

10

Turn

112 – 114

3

Beta strand

116 – 125

10

Helix

132 – 136

5

Beta strand

141 – 143

3

Helix

150 – 158

9

Beta strand

164 – 167

4

Helix

171 – 180

10

Beta strand

183 – 186

4

Helix

191 – 205

15

Beta strand

206 – 208

3

Helix

210 – 220

11

Helix

573 – 617

45

Helix

645 – 663

19

Helix

674 – 681

8

Helix

686 – 689

4

Helix

690 – 692

3

Turn

695 – 697

3

Helix

698 – 704

7

Helix

706 – 710

5

Beta strand

712 – 715

4

Helix

717 – 719

3

Helix

721 – 724

4

Beta strand

732 – 739

8

Beta strand

751 – 754

4

Beta strand

757 – 763

7

Beta strand

766 – 771

6

Helix

780 – 802

23

Turn

825 – 828

4

Beta strand

829 – 831

3

Helix

834 – 853

20

Sequences

	Sequence		Length	Mass (Da)
	P22523 [UniParc]. Last modified July 15, 1998. Version 2. Checksum: 38C7874BEB78D6D6	FASTA	1,486	170,230
	10 20 30 40 50 60 MIERGKFRSL TLINWNGFFA RTFDLDELVT TLSGGNGAGK STTMAAFVTA LIPDLTLLHF 70 80 90 100 110 120 RNTTEAGATS GSRDKGLHGK LKAGVCYSML DTINSRHQRV VVGVRLQQVA GRDRKVDIKP 130 140 150 160 170 180 FAIQGLPMSV QPTQLVTETL NERQARVLPL NELKDKLEAM EGVQFKQFNS ITDYHSLMFD 190 200 210 220 230 240 LGIIARRLRS ASDRSKFYRL IEASLYGGIS SAITRSLRDY LLPENSGVRK AFQDMEAALR 250 260 270 280 290 300 ENRMTLEAIR VTQSDRDLFK HLISEATNYV AADYMRHANE RRVHLDKALE FRRELHTSRQ 310 320 330 340 350 360 QLAAEQYKHV DMARELAEHN GAEGDLEADY QAASDHLNLV QTALRQQEKI ERYEADLDEL 370 380 390 400 410 420 QIRLEEQNEV VAEAIERQQE NEARAEAAEL EVDELKSQLA DYQQALDVQQ TRAIQYNQAI 430 440 450 460 470 480 AALNRAKELC HLPDLTADCA AEWLETFQAK ELEATEKMLS LEQKMSMAQT AHSQFEQAYQ 490 500 510 520 530 540 LVVAINGPLA RNEAWDVARE LLREGVDQRH LAEQVQPLRM RLSELEQRLR EQQEAERLLA 550 560 570 580 590 600 DFCKRQGKNF DIDELEALHQ ELEARIASLS DSVSNAREER MALRQEQEQL QSRIQSLMQR 610 620 630 640 650 660 APVWLAAQNS LNQLSEQCGE EFTSSQDVTE YLQQLLERER EAIVERDEVG ARKNAVDEEI 670 680 690 700 710 720 ERLSQPGGSE DQRLNALAER FGGVLLSEIY DDVSLEDAPY FSALYGPSRH AIVVPDLSQV 730 740 750 760 770 780 TEHLEGLTDC PEDLYLIEGD PQSFDDSVFS VDELEKAVVV KIADRQWRYS RFPEVPLFGR 790 800 810 820 830 840 AARESRIESL HAEREVLSER FATLSFDVQK TQRLHQAFSR FIGSHLAVAF ESDPEAEIRQ 850 860 870 880 890 900 LNSRRVELER ALSNHENDNQ QQRIQFEQAK EGVTALNRIL PRLNLLADDS LADRVDEIRE 910 920 930 940 950 960 RLDEAQEAAR FVQQFGNQLA KLEPIVSVLQ SDPEQFEQLK EDYAYSQQMQ RDARQQAFAL 970 980 990 1000 1010 1020 TEVVQRRAHF SYSDSAEMLS GNSDLNEKLR ERLEQAEAER TRAREALRGH AAQLSQYNQV 1030 1040 1050 1060 1070 1080 LASLKSSYDT KKELLNDLQR ELQDIGVRAD SGAEERARIR RDELHAQLSN NRSRRNQLEK 1090 1100 1110 1120 1130 1140 ALTFCEAEMD NLTRKLRKLE RDYFEMREQV VTAKAGWCAV MRMVKDNGVE RRLHRRELAY 1150 1160 1170 1180 1190 1200 LSADDLRSMS DKALGALRLA VADNEHLRDV LRMSEDPKRP ERKIQFFVAV YQHLRERIRQ 1210 1220 1230 1240 1250 1260 DIIRTDDPVE AIEQMEIELS RLTEELTSRE QKLAISSRSV ANIIRKTIQR EQNRIRMLNQ 1270 1280 1290 1300 1310 1320 GLQNVSFGQV NSVRLNVNVR ETHAMLLDVL SEQHEQHQDL FNSNRLTFSE ALAKLYQRLN 1330 1340 1350 1360 1370 1380 PQIDMGQRTP QTIGEELLDY RNYLEMEVEV NRGSDGWLRA ESGALSTGEA IGTGMSILVM 1390 1400 1410 1420 1430 1440 VVQSWEDESR RLRGKDISPC RLLFLDEAAR LDARSIATLF ELCERLQMQL IIAAPENISP 1450 1460 1470 1480 EKGTTYKLVR KVFQNTEHVH VVGLRGFAPQ LPETLPGTDE APSQAS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The new gene mukB codes for a 177 kd protein with coiled-coil domains involved in chromosome partitioning of E. coli." Niki H., Jaffe A., Imamura R., Ogura T., Hiraga S. EMBO J. 10:183-193(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"Two mutant alleles of mukB, a gene essential for chromosome partition in Escherichia coli." Yamanaka K., Mitani T., Feng J., Ogura T., Niki H., Hiraga S. FEMS Microbiol. Lett. 123:27-31(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANTS MUKB33 AND MUKB106.
[3]	"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." 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. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"New killing system controlled by two genes located immediately upstream of the mukB gene in Escherichia coli." Feng J., Yamanaka K., Niki H., Ogura T., Hiraga S. Mol. Gen. Genet. 243:136-147(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"Escherichia coli condensin MukB stimulates topoisomerase IV activity by a direct physical interaction." Li Y., Stewart N.K., Berger A.J., Vos S., Schoeffler A.J., Berger J.M., Chait B.T., Oakley M.G. Proc. Natl. Acad. Sci. U.S.A. 107:18832-18837(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 9-21; 41-61; 353-363 AND 681-709, MODIFIES FUNCTION OF TOPOISOMERASE IV, INTERACTION WITH MUKE; MUKF; ACP AND PARC, MUTAGENESIS OF GLU-688 AND ASP-692.
[8]	"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." Niki H., Imamura R., Kitaoka M., Yamanaka K., Ogura T., Hiraga S. EMBO J. 11:5101-5109(1992) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT.
[9]	"Interaction of the N-terminal domain of MukB with the bacterial tubulin homologue FtsZ." Lockhart A., Kendrick-Jones J. FEBS Lett. 430:278-282(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FTSZ.
[10]	"Complex formation of MukB, MukE and MukF proteins involved in chromosome partitioning in Escherichia coli." Yamazoe M., Onogi T., Sunako Y., Niki H., Yamanaka K., Ichimura T., Hiraga S. EMBO J. 18:5873-5884(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MUKE AND MUKF, MUTAGENESIS OF SER-33; LYS-40; ASP-1201; VAL-1381; LEU-1403; PHE-1404; ASP-1406; MET-1428 AND GLN-1429.
[11]	"Suppression of chromosome segregation defects of Escherichia coli muk mutants by mutations in topoisomerase I." Sawitzke J.A., Austin S. Proc. Natl. Acad. Sci. U.S.A. 97:1671-1676(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Distribution of the Escherichia coli structural maintenance of chromosomes (SMC)-like protein MukB in the cell." den Blaauwen T., Lindqvist A., Loewe J., Nanninga N. Mol. Microbiol. 42:1179-1188(2001) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[13]	"New partners of acyl carrier protein detected in Escherichia coli by tandem affinity purification." Gully D., Moinier D., Loiseau L., Bouveret E. FEBS Lett. 548:90-96(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH SPOT; ISCS AND ACP.
[14]	"Isolation and identification of new inner membrane-associated proteins that localize to cell poles in Escherichia coli." Li G., Young K.D. Mol. Microbiol. 84:276-295(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION. Strain: K12 / MG1655 / ATCC 47076.
[15]	"Crystal structure of the N-terminal domain of MukB: a protein involved in chromosome partitioning." van den Ent F., Lockhart A., Kendrick-Jones J., Loewe J. Structure 7:1181-1187(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-227.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X57550 Genomic DNA. Translation: CAA40776.1.
D31701 Genomic DNA. Translation: BAA06510.1.
U00096 Genomic DNA. Translation: AAC74010.1.
AP009048 Genomic DNA. Translation: BAA35670.1.
D26440 Genomic DNA. Translation: BAA05459.1.

PIR

C64832.
JH0228.

RefSeq

NP_415444.1. NC_000913.2.
YP_489196.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QHL	X-ray	2.20	A	1-227	[»]
2WMM	X-ray	2.30	A/B	645-804	[»]
3IBP	X-ray	3.10	A	566-863	[»]

ProteinModelPortal

P22523.

SMR

P22523. Positions 1-258, 572-854, 1234-1468.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10273N.

IntAct

P22523. 56 interactions.

MINT

MINT-1225884.

STRING

511145.b0924.

Proteomic databases

PaxDb

P22523.

PRIDE

P22523.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74010; AAC74010; b0924.
BAA35670; BAA35670; BAA35670.

GeneID

12932693.
945549.

KEGG

ecj:Y75_p0896.
eco:b0924.

PATRIC

32117061. VBIEscCol129921_0955.

Organism-specific databases

EchoBASE

EB0613.

EcoGene

EG10618. mukB.

Phylogenomic databases

eggNOG

COG3096.

HOGENOM

HOG000278243.

KO

K03632.

OMA

RELQEHN.

ProtClustDB

PRK04863.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10618-MONOMER.
ECOL316407:JW0907-MONOMER.

Gene expression databases

Genevestigator

P22523.

Family and domain databases

HAMAP

MF_01800. MukB.

InterPro

IPR012090. MukB.
IPR007406. MukB_N_dom.
[Graphical view]

Pfam

PF04310. MukB. 1 hit.
[Graphical view]

PIRSF

PIRSF005246. MukB. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P22523.

Entry information

Entry name

MUKB_ECOLI

Accession

Primary (citable) accession number: P22523
Secondary accession number(s): P71227, P77164, Q47398

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	July 15, 1998
Last modified:	May 1, 2013
This is version 139 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program