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Q9PLZ2 (TOP1_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA topoisomerase 1

EC=5.99.1.2
Alternative name(s):
DNA topoisomerase I
Omega-protein
Relaxing enzyme
Swivelase
Untwisting enzyme
Gene names
Name:topA
Ordered Locus Names:Cj1686c
OrganismCampylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168) [Reference proteome] [HAMAP]
Taxonomic identifier192222 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length700 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone By similarity. HAMAP-Rule MF_00952

Catalytic activity

ATP-independent breakage of single-stranded DNA, followed by passage and rejoining. HAMAP-Rule MF_00952

Cofactor

Magnesium. Binds two Mg2+ per subunit By similarity. HAMAP-Rule MF_00952

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00952

Sequence similarities

Belongs to the type IA topoisomerase family.

Contains 1 Toprim domain.

Ontologies

Keywords
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Magnesium
Metal-binding
Zinc
   Molecular functionIsomerase
Topoisomerase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA topological change

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentchromosome

Inferred from electronic annotation. Source: InterPro

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA topoisomerase type I activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 700700DNA topoisomerase 1 HAMAP-Rule MF_00952
PRO_0000145146

Regions

Domain3 – 114112Toprim
Zinc finger573 – 59927C4-type 1 HAMAP-Rule MF_00952
Zinc finger629 – 65628C4-type 2 HAMAP-Rule MF_00952
Zinc finger669 – 69224C4-type 3 HAMAP-Rule MF_00952
Region164 – 1696Interaction with DNA By similarity

Sites

Active site2981O-(5'-phospho-DNA)-tyrosine intermediate By similarity
Metal binding91Magnesium 1; catalytic By similarity
Metal binding831Magnesium 1; catalytic By similarity
Metal binding831Magnesium 2 By similarity
Metal binding851Magnesium 2 By similarity
Site331Interaction with DNA By similarity
Site1401Interaction with DNA By similarity
Site1411Interaction with DNA By similarity
Site1441Interaction with DNA By similarity
Site1491Interaction with DNA By similarity
Site3001Interaction with DNA By similarity
Site4851Interaction with DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PLZ2 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 86CE6DE6A8231A00

FASTA70079,148
        10         20         30         40         50         60 
MKKNLIIVES PAKAKTIGNF LGKDYEVIAS KGHIRDLPKS SFGIKIEDDE FIPEYRITSD 

        70         80         90        100        110        120 
HSALVKELKS KAKDAKEVYL ATDEDREGEA IAYHIAKAIG KDENTLPRIV FHEITKSAIE 

       130        140        150        160        170        180 
NALKNPRKLN MHSVNAQQTR RLLDRIVGYK LSPLLGQKIQ RGLSAGRVQS AALKIIVDRE 

       190        200        210        220        230        240 
KEIRAFVPLE YFSIDMIFQK DLDAELVEFD KAKIEKLTIT NKDRAKLILE ACKNEVYSIS 

       250        260        270        280        290        300 
DIESKERKIA PPPPFMTSTL QQSASNRLGF NPKKTMMIAQ KLYEGVNTHE GVMGVITYMR 

       310        320        330        340        350        360 
TDSLNLAKEA VENARKFIQA NFGKDYLPSK ANVYTTKTKG AQEAHEAIRP TNLSFTPEIA 

       370        380        390        400        410        420 
AKFLDKDELK LYTLIYNRFL ACQMSPAISQ TQNVFVKNDR VVFKISGRKI LFDGYYKVYG 

       430        440        450        460        470        480 
DMDKDKILPN FKIGQNLKVQ NLEMNSHFTE PPSRYSEAGL VKKLESLGIG RPSTYAPTIS 

       490        500        510        520        530        540 
ILTSRDYVTI DKKQLIPSDV AFNVTEVLEK NFSDIVDSKF TSNLENTLDE IAEDKADWQE 

       550        560        570        580        590        600 
TLKEFYYPFM RKIEEGKTKI ASQKTVTKLG ESCPDCGGEL AIRKGRFGEF VACLNFPKCK 

       610        620        630        640        650        660 
YSRNLKSESK NESENTAAKA KANGTGITCP SCQKGEIVER FSKRGKFYGC SAYPKCNFIS 

       670        680        690        700 
KYKPSEEKCE ECGETLVIKE LKKGTFLECL KCKIKKEMKD 

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References

[1]"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences."
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. expand/collapse author list , van Vliet A.H.M., Whitehead S., Barrell B.G.
Nature 403:665-668(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 11168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL111168 Genomic DNA. Translation: CAL35780.1.
PIRB81266.
RefSeqYP_002345052.1. NC_002163.1.

3D structure databases

ProteinModelPortalQ9PLZ2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING192222.Cj1686c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL35780; CAL35780; Cj1686c.
GeneID905960.
KEGGcje:Cj1686c.
PATRIC20060346. VBICamJej33762_1660.

Phylogenomic databases

eggNOGCOG0551.
HOGENOMHOG000004018.
KOK03168.
OMAVVECDKC.
OrthoDBEOG6S7XQ9.

Enzyme and pathway databases

BioCycCJEJ192222:GJTS-1652-MONOMER.

Family and domain databases

Gene3D1.10.460.10. 2 hits.
2.70.20.10. 2 hits.
3.40.50.140. 1 hit.
HAMAPMF_00952. Topoisom_1_prok.
InterProIPR000380. Topo_IA.
IPR003601. Topo_IA_2.
IPR023406. Topo_IA_AS.
IPR013497. Topo_IA_cen.
IPR013824. Topo_IA_cen_sub1.
IPR013825. Topo_IA_cen_sub2.
IPR023405. Topo_IA_core_domain.
IPR003602. Topo_IA_DNA-bd.
IPR013498. Topo_IA_Znf.
IPR005733. TopoI_bac-type.
IPR028612. Topoisom_1_IA.
IPR006171. Toprim_domain.
[Graphical view]
PANTHERPTHR11390. PTHR11390. 1 hit.
PfamPF01131. Topoisom_bac. 1 hit.
PF01751. Toprim. 1 hit.
PF01396. zf-C4_Topoisom. 2 hits.
[Graphical view]
PRINTSPR00417. PRTPISMRASEI.
SMARTSM00437. TOP1Ac. 1 hit.
SM00436. TOP1Bc. 1 hit.
SM00493. TOPRIM. 1 hit.
[Graphical view]
SUPFAMSSF56712. SSF56712. 1 hit.
TIGRFAMsTIGR01051. topA_bact. 1 hit.
PROSITEPS00396. TOPOISOMERASE_I_PROK. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTOP1_CAMJE
AccessionPrimary (citable) accession number: Q9PLZ2
Secondary accession number(s): Q0P7U5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families