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Protein

Chromosome partition protein MukB

Gene

mukB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi34 – 418ATPSequence analysis

GO - Molecular functioni

  • ATP binding Source: EcoCyc
  • DNA binding Source: EcoCyc
  • GTP binding Source: EcoCyc
  • identical protein binding Source: EcoCyc

GO - Biological processi

  • cell division Source: EcoCyc
  • chromosome condensation Source: EcoCyc
  • chromosome segregation Source: EcoliWiki
  • DNA replication Source: UniProtKB-HAMAP
  • sister chromatid cohesion Source: EcoliWiki
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Chromosome partition, DNA condensation

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10618-MONOMER.
ECOL316407:JW0907-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Chromosome partition protein MukB
Alternative name(s):
Structural maintenance of chromosome-related protein
Gene namesi
Name:mukB
Ordered Locus Names:b0924, JW0907
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10618. mukB.

Subcellular locationi

GO - Cellular componenti

  • condensin complex Source: EcoCyc
  • cytosol Source: EcoCyc
  • nucleoid Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi33 – 331S → F in mukB106; no effect. 1 Publication
Mutagenesisi40 – 401K → L: No effect. 1 Publication
Mutagenesisi688 – 6881E → A: Does not rescue a ts-mutant of MukB. 1 Publication
Mutagenesisi692 – 6921D → A: Does not rescue a ts-mutant of MukB; less binding of ParC. 1 Publication
Mutagenesisi1201 – 12011D → N in mukB33; no effect. 1 Publication
Mutagenesisi1381 – 13811V → L: Abolishes DNA-binding, but remains associated with MukE and MukF. 1 Publication
Mutagenesisi1403 – 14031L → P: Abolishes association with MukE and MukF, but still binds DNA. 1 Publication
Mutagenesisi1404 – 14041F → L: No effect. 1 Publication
Mutagenesisi1406 – 14061D → N: No effect. 1 Publication
Mutagenesisi1428 – 14281M → L: No effect. 1 Publication
Mutagenesisi1429 – 14291Q → R: Abolishes association with MukE and MukF, but still binds DNA. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14861486Chromosome partition protein MukBPRO_0000068214Add
BLAST

Proteomic databases

EPDiP22523.
PaxDbiP22523.
PRIDEiP22523.

Interactioni

Subunit structurei

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.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
parCP0AFI27EBI-542943,EBI-878544

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4261687. 376 interactions.
DIPiDIP-10273N.
IntActiP22523. 56 interactions.
MINTiMINT-1225884.
STRINGi511145.b0924.

Structurei

Secondary structure

1
1486
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 1510Combined sources
Beta strandi18 – 236Combined sources
Helixi25 – 339Combined sources
Helixi38 – 5114Combined sources
Turni55 – 573Combined sources
Helixi78 – 803Combined sources
Beta strandi83 – 9311Combined sources
Beta strandi99 – 10810Combined sources
Turni112 – 1143Combined sources
Beta strandi116 – 12510Combined sources
Helixi132 – 1365Combined sources
Beta strandi141 – 1433Combined sources
Helixi150 – 1589Combined sources
Beta strandi164 – 1674Combined sources
Helixi171 – 18010Combined sources
Beta strandi183 – 1864Combined sources
Helixi191 – 20515Combined sources
Beta strandi206 – 2083Combined sources
Helixi210 – 22011Combined sources
Helixi573 – 61745Combined sources
Helixi645 – 66319Combined sources
Helixi674 – 6818Combined sources
Helixi686 – 6894Combined sources
Helixi690 – 6923Combined sources
Turni695 – 6973Combined sources
Helixi698 – 7047Combined sources
Helixi706 – 7105Combined sources
Beta strandi712 – 7154Combined sources
Helixi717 – 7193Combined sources
Helixi721 – 7244Combined sources
Beta strandi732 – 7398Combined sources
Beta strandi743 – 7453Combined sources
Beta strandi751 – 7544Combined sources
Beta strandi757 – 7637Combined sources
Beta strandi766 – 7716Combined sources
Helixi780 – 80223Combined sources
Turni825 – 8284Combined sources
Beta strandi829 – 8313Combined sources
Helixi834 – 85320Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QHLX-ray2.20A1-227[»]
2WMMX-ray2.30A/B645-804[»]
3IBPX-ray3.10A566-863[»]
4MN4X-ray2.30C/D645-804[»]
ProteinModelPortaliP22523.
SMRiP22523. Positions 1-258, 572-854, 1234-1468.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22523.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni645 – 804160Sufficient for ParC bindingAdd
BLAST
Regioni666 – 783118Flexible hingeAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili326 – 41893Sequence analysisAdd
BLAST
Coiled coili444 – 48037Sequence analysisAdd
BLAST
Coiled coili509 – 60395Sequence analysisAdd
BLAST
Coiled coili835 – 92389Sequence analysisAdd
BLAST
Coiled coili977 – 1115139Sequence analysisAdd
BLAST
Coiled coili1209 – 126658Sequence analysisAdd
BLAST

Domaini

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.

Sequence similaritiesi

Belongs to the SMC family. MukB subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG4105DUC. Bacteria.
COG3096. LUCA.
HOGENOMiHOG000278243.
InParanoidiP22523.
KOiK03632.
OMAiDRCEEIR.
PhylomeDBiP22523.

Family and domain databases

HAMAPiMF_01800. MukB. 1 hit.
InterProiIPR012090. MukB.
IPR032520. MukB_hinge.
IPR007406. MukB_N_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF04310. MukB. 1 hit.
PF16330. MukB_hinge. 1 hit.
[Graphical view]
PIRSFiPIRSF005246. MukB. 1 hit.
SUPFAMiSSF52540. SSF52540. 3 hits.

Sequencei

Sequence statusi: Complete.

P22523-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIERGKFRSL TLINWNGFFA RTFDLDELVT TLSGGNGAGK STTMAAFVTA
60 70 80 90 100
LIPDLTLLHF RNTTEAGATS GSRDKGLHGK LKAGVCYSML DTINSRHQRV
110 120 130 140 150
VVGVRLQQVA GRDRKVDIKP FAIQGLPMSV QPTQLVTETL NERQARVLPL
160 170 180 190 200
NELKDKLEAM EGVQFKQFNS ITDYHSLMFD LGIIARRLRS ASDRSKFYRL
210 220 230 240 250
IEASLYGGIS SAITRSLRDY LLPENSGVRK AFQDMEAALR ENRMTLEAIR
260 270 280 290 300
VTQSDRDLFK HLISEATNYV AADYMRHANE RRVHLDKALE FRRELHTSRQ
310 320 330 340 350
QLAAEQYKHV DMARELAEHN GAEGDLEADY QAASDHLNLV QTALRQQEKI
360 370 380 390 400
ERYEADLDEL QIRLEEQNEV VAEAIERQQE NEARAEAAEL EVDELKSQLA
410 420 430 440 450
DYQQALDVQQ TRAIQYNQAI AALNRAKELC HLPDLTADCA AEWLETFQAK
460 470 480 490 500
ELEATEKMLS LEQKMSMAQT AHSQFEQAYQ LVVAINGPLA RNEAWDVARE
510 520 530 540 550
LLREGVDQRH LAEQVQPLRM RLSELEQRLR EQQEAERLLA DFCKRQGKNF
560 570 580 590 600
DIDELEALHQ ELEARIASLS DSVSNAREER MALRQEQEQL QSRIQSLMQR
610 620 630 640 650
APVWLAAQNS LNQLSEQCGE EFTSSQDVTE YLQQLLERER EAIVERDEVG
660 670 680 690 700
ARKNAVDEEI ERLSQPGGSE DQRLNALAER FGGVLLSEIY DDVSLEDAPY
710 720 730 740 750
FSALYGPSRH AIVVPDLSQV TEHLEGLTDC PEDLYLIEGD PQSFDDSVFS
760 770 780 790 800
VDELEKAVVV KIADRQWRYS RFPEVPLFGR AARESRIESL HAEREVLSER
810 820 830 840 850
FATLSFDVQK TQRLHQAFSR FIGSHLAVAF ESDPEAEIRQ LNSRRVELER
860 870 880 890 900
ALSNHENDNQ QQRIQFEQAK EGVTALNRIL PRLNLLADDS LADRVDEIRE
910 920 930 940 950
RLDEAQEAAR FVQQFGNQLA KLEPIVSVLQ SDPEQFEQLK EDYAYSQQMQ
960 970 980 990 1000
RDARQQAFAL TEVVQRRAHF SYSDSAEMLS GNSDLNEKLR ERLEQAEAER
1010 1020 1030 1040 1050
TRAREALRGH AAQLSQYNQV LASLKSSYDT KKELLNDLQR ELQDIGVRAD
1060 1070 1080 1090 1100
SGAEERARIR RDELHAQLSN NRSRRNQLEK ALTFCEAEMD NLTRKLRKLE
1110 1120 1130 1140 1150
RDYFEMREQV VTAKAGWCAV MRMVKDNGVE RRLHRRELAY LSADDLRSMS
1160 1170 1180 1190 1200
DKALGALRLA VADNEHLRDV LRMSEDPKRP ERKIQFFVAV YQHLRERIRQ
1210 1220 1230 1240 1250
DIIRTDDPVE AIEQMEIELS RLTEELTSRE QKLAISSRSV ANIIRKTIQR
1260 1270 1280 1290 1300
EQNRIRMLNQ GLQNVSFGQV NSVRLNVNVR ETHAMLLDVL SEQHEQHQDL
1310 1320 1330 1340 1350
FNSNRLTFSE ALAKLYQRLN PQIDMGQRTP QTIGEELLDY RNYLEMEVEV
1360 1370 1380 1390 1400
NRGSDGWLRA ESGALSTGEA IGTGMSILVM VVQSWEDESR RLRGKDISPC
1410 1420 1430 1440 1450
RLLFLDEAAR LDARSIATLF ELCERLQMQL IIAAPENISP EKGTTYKLVR
1460 1470 1480
KVFQNTEHVH VVGLRGFAPQ LPETLPGTDE APSQAS
Length:1,486
Mass (Da):170,230
Last modified:July 15, 1998 - v2
Checksum:i38C7874BEB78D6D6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti266 – 2661A → R in CAA40776 (PubMed:1989883).Curated
Sequence conflicti266 – 2661A → R in BAA06510 (PubMed:7988894).Curated
Sequence conflicti318 – 3192EH → DD in CAA40776 (PubMed:1989883).Curated
Sequence conflicti1134 – 11341H → D in CAA40776 (PubMed:1989883).Curated
Sequence conflicti1174 – 11752SE → VQ in CAA40776 (PubMed:1989883).Curated
Sequence conflicti1276 – 12772Missing in CAA40776 (PubMed:1989883).Curated
Sequence conflicti1276 – 12772Missing in BAA06510 (PubMed:7988894).Curated
Sequence conflicti1357 – 138024WLRAE…SILVM → CCAQSLVHCRPVRRWYRYVD SGV in CAA40776 (PubMed:1989883).CuratedAdd
BLAST
Sequence conflicti1390 – 148697RRLRG…PSQAS → AACAVKISLLAACCSSMKQR DWMLVLSPRCLNCVSVCKCN SSSQRRKISARRKAPPINWC VKSSRIPNTFMSSACEDLRR NSLKRFQELTKRLLRRVKIK QQCRLFFFRKLRFCTKKVAH YGALFFKLLYIRLCKNVRRL YTEDKPDE in CAA40776 (PubMed:1989883).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiC64832.
JH0228.
RefSeqiNP_415444.1. NC_000913.3.
WP_000572698.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74010; AAC74010; b0924.
BAA35670; BAA35670; BAA35670.
GeneIDi945549.
KEGGiecj:JW0907.
eco:b0924.
PATRICi32117061. VBIEscCol129921_0955.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiC64832.
JH0228.
RefSeqiNP_415444.1. NC_000913.3.
WP_000572698.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QHLX-ray2.20A1-227[»]
2WMMX-ray2.30A/B645-804[»]
3IBPX-ray3.10A566-863[»]
4MN4X-ray2.30C/D645-804[»]
ProteinModelPortaliP22523.
SMRiP22523. Positions 1-258, 572-854, 1234-1468.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261687. 376 interactions.
DIPiDIP-10273N.
IntActiP22523. 56 interactions.
MINTiMINT-1225884.
STRINGi511145.b0924.

Proteomic databases

EPDiP22523.
PaxDbiP22523.
PRIDEiP22523.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74010; AAC74010; b0924.
BAA35670; BAA35670; BAA35670.
GeneIDi945549.
KEGGiecj:JW0907.
eco:b0924.
PATRICi32117061. VBIEscCol129921_0955.

Organism-specific databases

EchoBASEiEB0613.
EcoGeneiEG10618. mukB.

Phylogenomic databases

eggNOGiENOG4105DUC. Bacteria.
COG3096. LUCA.
HOGENOMiHOG000278243.
InParanoidiP22523.
KOiK03632.
OMAiDRCEEIR.
PhylomeDBiP22523.

Enzyme and pathway databases

BioCyciEcoCyc:EG10618-MONOMER.
ECOL316407:JW0907-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP22523.
PROiP22523.

Family and domain databases

HAMAPiMF_01800. MukB. 1 hit.
InterProiIPR012090. MukB.
IPR032520. MukB_hinge.
IPR007406. MukB_N_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF04310. MukB. 1 hit.
PF16330. MukB_hinge. 1 hit.
[Graphical view]
PIRSFiPIRSF005246. MukB. 1 hit.
SUPFAMiSSF52540. SSF52540. 3 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiMUKB_ECOLI
AccessioniPrimary (citable) accession number: P22523
Secondary accession number(s): P71227, P77164, Q47398
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: July 15, 1998
Last modified: September 7, 2016
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.