REP_ECOLI
ID REP_ECOLI Reviewed; 673 AA.
AC P09980; Q2M886; Q6BF05;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=ATP-dependent DNA helicase Rep {ECO:0000255|HAMAP-Rule:MF_01920};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01920};
GN Name=rep {ECO:0000255|HAMAP-Rule:MF_01920};
GN OrderedLocusNames=b3778, JW5604;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3029683; DOI=10.1093/nar/15.2.465;
RA Gilchrist C.A., Denhardt D.T.;
RT "Escherichia coli rep gene: sequence of the gene, the encoded helicase, and
RT its homology with uvrD.";
RL Nucleic Acids Res. 15:465-475(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP SEQUENCE REVISION TO 196.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
RX PubMed=2999067; DOI=10.1128/jb.164.3.1004-1010.1985;
RA Bialkowska-Hobrzanska H., Gilchrist C.A., Denhardt D.T.;
RT "Escherichia coli rep gene: identification of the promoter and N terminus
RT of the rep protein.";
RL J. Bacteriol. 164:1004-1010(1985).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND DNA-BINDING.
RX PubMed=221901; DOI=10.1073/pnas.76.4.1658;
RA Yarranton G.T., Gefter M.L.;
RT "Enzyme-catalyzed DNA unwinding: studies on Escherichia coli rep protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 76:1658-1662(1979).
RN [8]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=1658335; DOI=10.1016/0022-2836(91)90926-w;
RA Chao K.L., Lohman T.M.;
RT "DNA-induced dimerization of the Escherichia coli Rep helicase.";
RL J. Mol. Biol. 221:1165-1181(1991).
RN [9]
RP ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=11428893; DOI=10.1006/jmbi.2001.4758;
RA Cheng W., Hsieh J., Brendza K.M., Lohman T.M.;
RT "E. coli Rep oligomers are required to initiate DNA unwinding in vitro.";
RL J. Mol. Biol. 310:327-350(2001).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-640.
RX PubMed=9288744; DOI=10.1016/s0092-8674(00)80525-5;
RA Korolev S., Hsieh J., Gauss G.H., Lohman T.M., Waksman G.;
RT "Major domain swiveling revealed by the crystal structures of complexes of
RT E. coli Rep helicase bound to single-stranded DNA and ADP.";
RL Cell 90:635-647(1997).
CC -!- FUNCTION: Rep helicase is a single-stranded DNA-dependent ATPase
CC involved in DNA replication; it can initiate unwinding at a nick in the
CC DNA. It binds to the single-stranded DNA and acts in a progressive
CC fashion along the DNA in the 3' to 5' direction. {ECO:0000255|HAMAP-
CC Rule:MF_01920, ECO:0000269|PubMed:221901}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01920,
CC ECO:0000269|PubMed:1658335, ECO:0000269|PubMed:221901};
CC -!- ACTIVITY REGULATION: Binding to DNA induces dimerization, which is
CC required for DNA helicase activity. {ECO:0000269|PubMed:11428893,
CC ECO:0000269|PubMed:1658335}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01920,
CC ECO:0000269|PubMed:11428893, ECO:0000269|PubMed:1658335}.
CC -!- INTERACTION:
CC P09980; P0ACB0: dnaB; NbExp=3; IntAct=EBI-6558011, EBI-548978;
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01920}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA28481.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X04794; CAA28481.1; ALT_FRAME; Genomic_DNA.
DR EMBL; M87049; AAA67579.1; -; Genomic_DNA.
DR EMBL; U00096; AAT48209.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77520.1; -; Genomic_DNA.
DR EMBL; M11055; AAA24518.1; -; Genomic_DNA.
DR PIR; E65181; HJECDR.
DR RefSeq; WP_001238899.1; NZ_LN832404.1.
DR RefSeq; YP_026251.1; NC_000913.3.
DR PDB; 1UAA; X-ray; 3.00 A; A/B=1-673.
DR PDBsum; 1UAA; -.
DR AlphaFoldDB; P09980; -.
DR SMR; P09980; -.
DR BioGRID; 4263317; 69.
DR BioGRID; 852591; 3.
DR ComplexPortal; CPX-1953; Replication restart pre-primosome complex priC-rep variant.
DR ComplexPortal; CPX-5911; Replication restart primosome complex, priC-rep variant.
DR DIP; DIP-10662N; -.
DR IntAct; P09980; 4.
DR STRING; 511145.b3778; -.
DR jPOST; P09980; -.
DR PaxDb; P09980; -.
DR PRIDE; P09980; -.
DR EnsemblBacteria; AAT48209; AAT48209; b3778.
DR EnsemblBacteria; BAE77520; BAE77520; BAE77520.
DR GeneID; 948292; -.
DR KEGG; ecj:JW5604; -.
DR KEGG; eco:b3778; -.
DR PATRIC; fig|511145.12.peg.3893; -.
DR EchoBASE; EB0830; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_5_4_6; -.
DR InParanoid; P09980; -.
DR OMA; HCANILI; -.
DR PhylomeDB; P09980; -.
DR BioCyc; EcoCyc:EG10837-MON; -.
DR BioCyc; MetaCyc:EG10837-MON; -.
DR EvolutionaryTrace; P09980; -.
DR PRO; PR:P09980; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:1990160; C:DnaB-DnaC-Rep-PriC complex; IC:ComplexPortal.
DR GO; GO:1990077; C:primosome complex; IC:ComplexPortal.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IDA:EcoCyc.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044787; P:bacterial-type DNA replication; IMP:EcoCyc.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IC:ComplexPortal.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IDA:EcoCyc.
DR GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
DR GO; GO:0031297; P:replication fork processing; IC:ComplexPortal.
DR GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_01920; Helicase_Rep; 1.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR005752; Helicase_Rep.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070; PTHR11070; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01074; rep; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA replication; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..673
FT /note="ATP-dependent DNA helicase Rep"
FT /id="PRO_0000102068"
FT DOMAIN 1..280
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01920"
FT DOMAIN 281..562
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01920"
FT BINDING 22..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01920"
FT BINDING 278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01920"
FT CONFLICT 73
FT /note="R -> H (in Ref. 1; CAA28481)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="A -> Q (in Ref. 1; CAA28481)"
FT /evidence="ECO:0000305"
FT CONFLICT 163..165
FT /note="IFA -> LLL (in Ref. 1; CAA28481)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="R -> A (in Ref. 2; AAA67579)"
FT /evidence="ECO:0000305"
FT CONFLICT 202..203
FT /note="KR -> NG (in Ref. 1; CAA28481)"
FT /evidence="ECO:0000305"
FT HELIX 5..12
FT /evidence="ECO:0007829|PDB:1UAA"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 28..43
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1UAA"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 57..70
FT /evidence="ECO:0007829|PDB:1UAA"
FT TURN 73..78
FT /evidence="ECO:0007829|PDB:1UAA"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 84..98
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 110..120
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 129..143
FT /evidence="ECO:0007829|PDB:1UAA"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 159..178
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 183..196
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 198..205
FT /evidence="ECO:0007829|PDB:1UAA"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:1UAA"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:1UAA"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 257..264
FT /evidence="ECO:0007829|PDB:1UAA"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:1UAA"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 281..292
FT /evidence="ECO:0007829|PDB:1UAA"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:1UAA"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 320..338
FT /evidence="ECO:0007829|PDB:1UAA"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:1UAA"
FT STRAND 345..352
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 358..364
FT /evidence="ECO:0007829|PDB:1UAA"
FT STRAND 369..372
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 381..394
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 399..405
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 415..427
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 432..435
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 441..444
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 448..467
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 471..482
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 484..491
FT /evidence="ECO:0007829|PDB:1UAA"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 495..516
FT /evidence="ECO:0007829|PDB:1UAA"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 527..535
FT /evidence="ECO:0007829|PDB:1UAA"
FT STRAND 551..557
FT /evidence="ECO:0007829|PDB:1UAA"
FT TURN 558..560
FT /evidence="ECO:0007829|PDB:1UAA"
FT STRAND 565..570
FT /evidence="ECO:0007829|PDB:1UAA"
FT STRAND 574..576
FT /evidence="ECO:0007829|PDB:1UAA"
FT TURN 577..580
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 581..584
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 590..601
FT /evidence="ECO:0007829|PDB:1UAA"
FT STRAND 603..611
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 617..619
FT /evidence="ECO:0007829|PDB:1UAA"
FT HELIX 628..632
FT /evidence="ECO:0007829|PDB:1UAA"
FT TURN 635..637
FT /evidence="ECO:0007829|PDB:1UAA"
SQ SEQUENCE 673 AA; 77024 MW; 3338B3399C668E3E CRC64;
MRLNPGQQQA VEFVTGPCLV LAGAGSGKTR VITNKIAHLI RGCGYQARHI AAVTFTNKAA
REMKERVGQT LGRKEARGLM ISTFHTLGLD IIKREYAALG MKANFSLFDD TDQLALLKEL
TEGLIEDDKV LLQQLISTIS NWKNDLKTPS QAAASAIGER DRIFAHCYGL YDAHLKACNV
LDFDDLILLP TLLLQRNEEV RKRWQNKIRY LLVDEYQDTN TSQYELVKLL VGSRARFTVV
GDDDQSIYSW RGARPQNLVL LSQDFPALKV IKLEQNYRSS GRILKAANIL IANNPHVFEK
RLFSELGYGA ELKVLSANNE EHEAERVTGE LIAHHFVNKT QYKDYAILYR GNHQSRVFEK
FLMQNRIPYK ISGGTSFFSR PEIKDLLAYL RVLTNPDDDS AFLRIVNTPK REIGPATLKK
LGEWAMTRNK SMFTASFDMG LSQTLSGRGY EALTRFTHWL AEIQRLAERE PIAAVRDLIH
GMDYESWLYE TSPSPKAAEM RMKNVNQLFS WMTEMLEGSE LDEPMTLTQV VTRFTLRDMM
ERGESEEELD QVQLMTLHAS KGLEFPYVYM VGMEEGFLPH QSSIDEDNID EERRLAYVGI
TRAQKELTFT LCKERRQYGE LVRPEPSRFL LELPQDDLIW EQERKVVSAE ERMQKGQSHL
ANLKAMMAAK RGK
