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Protein

ATP-dependent DNA helicase Rep

Gene

rep

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

Functioni

Rep helicase is a single-stranded DNA-dependent ATPase involved in DNA replication; it can initiate unwinding at a nick in the DNA. It binds to the single-stranded DNA and acts in a progressive fashion along the DNA in the 3' to 5' direction.UniRule annotation1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.UniRule annotation2 Publications

Enzyme regulationi

Binding to DNA induces dimerization, which is required for DNA helicase activity.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei278 – 2781ATPUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi22 – 298ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

  • bacterial-type DNA replication Source: EcoCyc
  • DNA unwinding involved in DNA replication Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10837-MONOMER.
ECOL316407:JW5604-MONOMER.
MetaCyc:EG10837-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent DNA helicase RepUniRule annotation (EC:3.6.4.12UniRule annotation)
Gene namesi
Name:repUniRule annotation
Ordered Locus Names:b3778, JW5604
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10837. rep.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 673673ATP-dependent DNA helicase RepPRO_0000102068Add
BLAST

Proteomic databases

PaxDbiP09980.
PRIDEiP09980.

Interactioni

Subunit structurei

Homodimer.UniRule annotation2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
dnaBP0ACB03EBI-6558011,EBI-548978

Protein-protein interaction databases

BioGridi4263317. 66 interactions.
DIPiDIP-10662N.
IntActiP09980. 4 interactions.
MINTiMINT-1286362.
STRINGi511145.b3778.

Structurei

Secondary structure

1
673
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 128Combined sources
Beta strandi15 – 206Combined sources
Helixi28 – 4316Combined sources
Helixi47 – 493Combined sources
Beta strandi50 – 567Combined sources
Helixi57 – 7014Combined sources
Turni73 – 786Combined sources
Beta strandi79 – 835Combined sources
Helixi84 – 9815Combined sources
Helixi110 – 12011Combined sources
Helixi129 – 14315Combined sources
Turni144 – 1463Combined sources
Helixi151 – 1544Combined sources
Helixi159 – 17820Combined sources
Helixi183 – 19614Combined sources
Helixi198 – 2058Combined sources
Beta strandi209 – 2146Combined sources
Helixi216 – 2183Combined sources
Helixi221 – 23111Combined sources
Turni232 – 2343Combined sources
Beta strandi237 – 2404Combined sources
Helixi243 – 2453Combined sources
Helixi249 – 2513Combined sources
Helixi257 – 2648Combined sources
Beta strandi269 – 2713Combined sources
Beta strandi276 – 2794Combined sources
Helixi281 – 29212Combined sources
Beta strandi304 – 3063Combined sources
Beta strandi312 – 3165Combined sources
Helixi320 – 33819Combined sources
Turni342 – 3443Combined sources
Beta strandi345 – 3528Combined sources
Helixi353 – 3553Combined sources
Helixi358 – 3647Combined sources
Beta strandi369 – 3724Combined sources
Helixi377 – 3793Combined sources
Helixi381 – 39414Combined sources
Helixi399 – 4057Combined sources
Helixi415 – 42713Combined sources
Helixi432 – 4354Combined sources
Helixi441 – 4444Combined sources
Helixi448 – 46720Combined sources
Helixi471 – 48212Combined sources
Helixi484 – 4918Combined sources
Beta strandi492 – 4943Combined sources
Helixi495 – 51622Combined sources
Beta strandi520 – 5223Combined sources
Helixi527 – 5359Combined sources
Beta strandi551 – 5577Combined sources
Turni558 – 5603Combined sources
Beta strandi565 – 5706Combined sources
Beta strandi574 – 5763Combined sources
Turni577 – 5804Combined sources
Helixi581 – 5844Combined sources
Helixi590 – 60112Combined sources
Beta strandi603 – 6119Combined sources
Helixi617 – 6193Combined sources
Helixi628 – 6325Combined sources
Turni635 – 6373Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UAAX-ray3.00A/B1-673[»]
ProteinModelPortaliP09980.
SMRiP09980. Positions 2-640.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09980.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 280280UvrD-like helicase ATP-bindingUniRule annotationAdd
BLAST
Domaini281 – 562282UvrD-like helicase C-terminalUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the helicase family. UvrD subfamily.UniRule annotation
Contains 1 uvrD-like helicase ATP-binding domain.UniRule annotation
Contains 1 uvrD-like helicase C-terminal domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C4R. Bacteria.
COG0210. LUCA.
HOGENOMiHOG000033015.
InParanoidiP09980.
KOiK03656.
OMAiEKVLMQN.
OrthoDBiEOG64N9TW.
PhylomeDBiP09980.

Family and domain databases

Gene3Di1.10.10.160. 1 hit.
3.40.50.300. 4 hits.
HAMAPiMF_01920. Helicase_Rep.
InterProiIPR013986. DExx_box_DNA_helicase_dom.
IPR014017. DNA_helicase_UvrD-like_C.
IPR000212. DNA_helicase_UvrD/REP.
IPR005752. Helicase_Rep.
IPR027417. P-loop_NTPase.
IPR014016. UvrD-like_ATP-bd.
[Graphical view]
PANTHERiPTHR11070. PTHR11070. 1 hit.
PfamiPF00580. UvrD-helicase. 1 hit.
PF13361. UvrD_C. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01074. rep. 1 hit.
PROSITEiPS51198. UVRD_HELICASE_ATP_BIND. 1 hit.
PS51217. UVRD_HELICASE_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P09980-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLNPGQQQA VEFVTGPCLV LAGAGSGKTR VITNKIAHLI RGCGYQARHI
60 70 80 90 100
AAVTFTNKAA REMKERVGQT LGRKEARGLM ISTFHTLGLD IIKREYAALG
110 120 130 140 150
MKANFSLFDD TDQLALLKEL TEGLIEDDKV LLQQLISTIS NWKNDLKTPS
160 170 180 190 200
QAAASAIGER DRIFAHCYGL YDAHLKACNV LDFDDLILLP TLLLQRNEEV
210 220 230 240 250
RKRWQNKIRY LLVDEYQDTN TSQYELVKLL VGSRARFTVV GDDDQSIYSW
260 270 280 290 300
RGARPQNLVL LSQDFPALKV IKLEQNYRSS GRILKAANIL IANNPHVFEK
310 320 330 340 350
RLFSELGYGA ELKVLSANNE EHEAERVTGE LIAHHFVNKT QYKDYAILYR
360 370 380 390 400
GNHQSRVFEK FLMQNRIPYK ISGGTSFFSR PEIKDLLAYL RVLTNPDDDS
410 420 430 440 450
AFLRIVNTPK REIGPATLKK LGEWAMTRNK SMFTASFDMG LSQTLSGRGY
460 470 480 490 500
EALTRFTHWL AEIQRLAERE PIAAVRDLIH GMDYESWLYE TSPSPKAAEM
510 520 530 540 550
RMKNVNQLFS WMTEMLEGSE LDEPMTLTQV VTRFTLRDMM ERGESEEELD
560 570 580 590 600
QVQLMTLHAS KGLEFPYVYM VGMEEGFLPH QSSIDEDNID EERRLAYVGI
610 620 630 640 650
TRAQKELTFT LCKERRQYGE LVRPEPSRFL LELPQDDLIW EQERKVVSAE
660 670
ERMQKGQSHL ANLKAMMAAK RGK
Length:673
Mass (Da):77,024
Last modified:October 11, 2004 - v3
Checksum:i3338B3399C668E3E
GO

Sequence cautioni

The sequence CAA28481.1 differs from that shown. Reason: Frameshift at positions 620 and 657. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731R → H in CAA28481 (PubMed:3029683).Curated
Sequence conflicti76 – 761A → Q in CAA28481 (PubMed:3029683).Curated
Sequence conflicti163 – 1653IFA → LLL in CAA28481 (PubMed:3029683).Curated
Sequence conflicti196 – 1961R → A in AAA67579 (PubMed:1379743).Curated
Sequence conflicti202 – 2032KR → NG in CAA28481 (PubMed:3029683).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04794 Genomic DNA. Translation: CAA28481.1. Frameshift.
M87049 Genomic DNA. Translation: AAA67579.1.
U00096 Genomic DNA. Translation: AAT48209.1.
AP009048 Genomic DNA. Translation: BAE77520.1.
M11055 Genomic DNA. Translation: AAA24518.1.
PIRiE65181. HJECDR.
RefSeqiWP_001238899.1. NZ_LN832404.1.
YP_026251.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAT48209; AAT48209; b3778.
BAE77520; BAE77520; BAE77520.
GeneIDi948292.
KEGGiecj:JW5604.
eco:b3778.
PATRICi32123047. VBIEscCol129921_3893.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04794 Genomic DNA. Translation: CAA28481.1. Frameshift.
M87049 Genomic DNA. Translation: AAA67579.1.
U00096 Genomic DNA. Translation: AAT48209.1.
AP009048 Genomic DNA. Translation: BAE77520.1.
M11055 Genomic DNA. Translation: AAA24518.1.
PIRiE65181. HJECDR.
RefSeqiWP_001238899.1. NZ_LN832404.1.
YP_026251.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UAAX-ray3.00A/B1-673[»]
ProteinModelPortaliP09980.
SMRiP09980. Positions 2-640.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263317. 66 interactions.
DIPiDIP-10662N.
IntActiP09980. 4 interactions.
MINTiMINT-1286362.
STRINGi511145.b3778.

Proteomic databases

PaxDbiP09980.
PRIDEiP09980.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT48209; AAT48209; b3778.
BAE77520; BAE77520; BAE77520.
GeneIDi948292.
KEGGiecj:JW5604.
eco:b3778.
PATRICi32123047. VBIEscCol129921_3893.

Organism-specific databases

EchoBASEiEB0830.
EcoGeneiEG10837. rep.

Phylogenomic databases

eggNOGiENOG4105C4R. Bacteria.
COG0210. LUCA.
HOGENOMiHOG000033015.
InParanoidiP09980.
KOiK03656.
OMAiEKVLMQN.
OrthoDBiEOG64N9TW.
PhylomeDBiP09980.

Enzyme and pathway databases

BioCyciEcoCyc:EG10837-MONOMER.
ECOL316407:JW5604-MONOMER.
MetaCyc:EG10837-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP09980.
PROiP09980.

Family and domain databases

Gene3Di1.10.10.160. 1 hit.
3.40.50.300. 4 hits.
HAMAPiMF_01920. Helicase_Rep.
InterProiIPR013986. DExx_box_DNA_helicase_dom.
IPR014017. DNA_helicase_UvrD-like_C.
IPR000212. DNA_helicase_UvrD/REP.
IPR005752. Helicase_Rep.
IPR027417. P-loop_NTPase.
IPR014016. UvrD-like_ATP-bd.
[Graphical view]
PANTHERiPTHR11070. PTHR11070. 1 hit.
PfamiPF00580. UvrD-helicase. 1 hit.
PF13361. UvrD_C. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01074. rep. 1 hit.
PROSITEiPS51198. UVRD_HELICASE_ATP_BIND. 1 hit.
PS51217. UVRD_HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Escherichia coli rep gene: sequence of the gene, the encoded helicase, and its homology with uvrD."
    Gilchrist C.A., Denhardt D.T.
    Nucleic Acids Res. 15:465-475(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes."
    Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.
    Science 257:771-778(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: SEQUENCE REVISION TO 196.
  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. "Escherichia coli rep gene: identification of the promoter and N terminus of the rep protein."
    Bialkowska-Hobrzanska H., Gilchrist C.A., Denhardt D.T.
    J. Bacteriol. 164:1004-1010(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
  7. "Enzyme-catalyzed DNA unwinding: studies on Escherichia coli rep protein."
    Yarranton G.T., Gefter M.L.
    Proc. Natl. Acad. Sci. U.S.A. 76:1658-1662(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, DNA-BINDING.
  8. "DNA-induced dimerization of the Escherichia coli Rep helicase."
    Chao K.L., Lohman T.M.
    J. Mol. Biol. 221:1165-1181(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT.
  9. "E. coli Rep oligomers are required to initiate DNA unwinding in vitro."
    Cheng W., Hsieh J., Brendza K.M., Lohman T.M.
    J. Mol. Biol. 310:327-350(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, SUBUNIT.
  10. "Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP."
    Korolev S., Hsieh J., Gauss G.H., Lohman T.M., Waksman G.
    Cell 90:635-647(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-640.

Entry informationi

Entry nameiREP_ECOLI
AccessioniPrimary (citable) accession number: P09980
Secondary accession number(s): Q2M886, Q6BF05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 11, 2004
Last modified: April 13, 2016
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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.