RECQ_ECOLI
ID RECQ_ECOLI Reviewed; 609 AA.
AC P15043; P76762; Q2M8C7; Q6BEZ3;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=ATP-dependent DNA helicase RecQ;
DE EC=3.6.4.12;
GN Name=recQ; OrderedLocusNames=b3822, JW5855;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3027506; DOI=10.1007/bf00430442;
RA Irino N., Nakayama K., Nakayama H.;
RT "The recQ gene of Escherichia coli K12: primary structure and evidence for
RT SOS regulation.";
RL Mol. Gen. Genet. 205:298-304(1986).
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], AND SEQUENCE REVISION TO
RP 254.
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 503-504.
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 FUNCTION, AND PROTEIN SEQUENCE OF 2-6.
RX PubMed=2164680; DOI=10.1073/pnas.87.14.5363;
RA Umezu K., Nakayama K., Nakayama H.;
RT "Escherichia coli RecQ protein is a DNA helicase.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:5363-5367(1990).
CC -!- FUNCTION: Involved in the RecF recombination pathway; its gene
CC expression is under the regulation of the SOS system. It is a DNA
CC helicase. {ECO:0000269|PubMed:2164680}.
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 -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA24517.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAA67618.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M30198; AAA24517.1; ALT_INIT; Genomic_DNA.
DR EMBL; M87049; AAA67618.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAT48221.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77479.1; -; Genomic_DNA.
DR RefSeq; WP_000035581.1; NZ_SSZK01000046.1.
DR RefSeq; YP_026263.3; NC_000913.3.
DR PDB; 1OYW; X-ray; 1.80 A; A=1-522.
DR PDB; 1OYY; X-ray; 2.50 A; A=1-523.
DR PDB; 1WUD; X-ray; 2.20 A; A/B/D=524-609.
DR PDBsum; 1OYW; -.
DR PDBsum; 1OYY; -.
DR PDBsum; 1WUD; -.
DR AlphaFoldDB; P15043; -.
DR SMR; P15043; -.
DR BioGRID; 4259619; 148.
DR DIP; DIP-10656N; -.
DR IntAct; P15043; 12.
DR STRING; 511145.b3822; -.
DR DrugBank; DB02930; Adenosine 5'-[gamma-thio]triphosphate.
DR PaxDb; P15043; -.
DR PRIDE; P15043; -.
DR EnsemblBacteria; AAT48221; AAT48221; b3822.
DR EnsemblBacteria; BAE77479; BAE77479; BAE77479.
DR GeneID; 58462160; -.
DR GeneID; 948318; -.
DR KEGG; ecj:JW5855; -.
DR KEGG; eco:b3822; -.
DR PATRIC; fig|511145.12.peg.3938; -.
DR EchoBASE; EB0826; -.
DR eggNOG; COG0514; Bacteria.
DR HOGENOM; CLU_001103_14_3_6; -.
DR InParanoid; P15043; -.
DR OMA; HHDIPKS; -.
DR PhylomeDB; P15043; -.
DR BioCyc; EcoCyc:EG10833-MON; -.
DR BioCyc; MetaCyc:EG10833-MON; -.
DR BRENDA; 3.6.4.12; 2026.
DR EvolutionaryTrace; P15043; -.
DR PRO; PR:P15043; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0043590; C:bacterial nucleoid; IDA:UniProtKB.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0030894; C:replisome; IDA:UniProtKB.
DR GO; GO:0017117; C:single-stranded DNA-dependent ATP-dependent DNA helicase complex; IDA:EcoliWiki.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:EcoliWiki.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:EcoliWiki.
DR GO; GO:0003677; F:DNA binding; IDA:EcoliWiki.
DR GO; GO:0003678; F:DNA helicase activity; IDA:EcoliWiki.
DR GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IDA:EcoliWiki.
DR GO; GO:0046914; F:transition metal ion binding; IDA:EcoliWiki.
DR GO; GO:0008270; F:zinc ion binding; IMP:EcoliWiki.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IGI:EcoliWiki.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IDA:EcoliWiki.
DR GO; GO:0006281; P:DNA repair; IGI:EcoliWiki.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.150.80; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR006293; DNA_helicase_ATP-dep_RecQ_bac.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR002121; HRDC_dom.
DR InterPro; IPR044876; HRDC_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR018982; RQC_domain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00570; HRDC; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR Pfam; PF09382; RQC; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00341; HRDC; 1.
DR SMART; SM00956; RQC; 1.
DR SUPFAM; SSF47819; SSF47819; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR01389; recQ; 1.
DR TIGRFAMs; TIGR00614; recQ_fam; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50967; HRDC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Reference proteome; SOS response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2164680"
FT CHAIN 2..609
FT /note="ATP-dependent DNA helicase RecQ"
FT /id="PRO_0000205033"
FT DOMAIN 34..202
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 223..371
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 529..609
FT /note="HRDC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00328"
FT MOTIF 146..149
FT /note="DEAH box"
FT BINDING 47..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 255
FT /note="R -> A (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 503..504
FT /note="RG -> A (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 600
FT /note="R -> P (in Ref. 1; AAA24517)"
FT /evidence="ECO:0000305"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:1OYW"
FT HELIX 30..38
FT /evidence="ECO:0007829|PDB:1OYW"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:1OYW"
FT HELIX 50..63
FT /evidence="ECO:0007829|PDB:1OYW"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:1OYW"
FT HELIX 75..87
FT /evidence="ECO:0007829|PDB:1OYW"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:1OYW"
FT HELIX 101..112
FT /evidence="ECO:0007829|PDB:1OYW"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:1OYW"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:1OYW"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1OYY"
FT HELIX 131..135
FT /evidence="ECO:0007829|PDB:1OYW"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:1OYW"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:1OYW"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:1OYW"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:1OYW"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:1OYW"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:1OYW"
FT HELIX 186..196
FT /evidence="ECO:0007829|PDB:1OYW"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:1OYW"
FT STRAND 213..219
FT /evidence="ECO:0007829|PDB:1OYW"
FT HELIX 223..233
FT /evidence="ECO:0007829|PDB:1OYW"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:1OYW"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:1OYW"
FT HELIX 246..258
FT /evidence="ECO:0007829|PDB:1OYW"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:1OYW"
FT HELIX 272..283
FT /evidence="ECO:0007829|PDB:1OYW"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:1OYW"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:1OYW"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:1OYW"
FT HELIX 317..324
FT /evidence="ECO:0007829|PDB:1OYW"
FT STRAND 334..340
FT /evidence="ECO:0007829|PDB:1OYW"
FT HELIX 342..353
FT /evidence="ECO:0007829|PDB:1OYW"
FT HELIX 359..375
FT /evidence="ECO:0007829|PDB:1OYW"
FT HELIX 381..388
FT /evidence="ECO:0007829|PDB:1OYW"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:1OYY"
FT HELIX 401..404
FT /evidence="ECO:0007829|PDB:1OYW"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:1OYW"
FT HELIX 413..425
FT /evidence="ECO:0007829|PDB:1OYW"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:1OYW"
FT HELIX 432..440
FT /evidence="ECO:0007829|PDB:1OYW"
FT HELIX 445..449
FT /evidence="ECO:0007829|PDB:1OYW"
FT HELIX 452..454
FT /evidence="ECO:0007829|PDB:1OYW"
FT TURN 456..463
FT /evidence="ECO:0007829|PDB:1OYW"
FT HELIX 466..478
FT /evidence="ECO:0007829|PDB:1OYW"
FT STRAND 481..484
FT /evidence="ECO:0007829|PDB:1OYW"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:1OYW"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:1OYW"
FT HELIX 496..498
FT /evidence="ECO:0007829|PDB:1OYW"
FT HELIX 499..502
FT /evidence="ECO:0007829|PDB:1OYW"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:1OYW"
FT HELIX 533..550
FT /evidence="ECO:0007829|PDB:1WUD"
FT HELIX 554..557
FT /evidence="ECO:0007829|PDB:1WUD"
FT HELIX 560..569
FT /evidence="ECO:0007829|PDB:1WUD"
FT HELIX 574..578
FT /evidence="ECO:0007829|PDB:1WUD"
FT HELIX 585..603
FT /evidence="ECO:0007829|PDB:1WUD"
SQ SEQUENCE 609 AA; 68364 MW; 82542DE445655D48 CRC64;
MAQAEVLNLE SGAKQVLQET FGYQQFRPGQ EEIIDTVLSG RDCLVVMPTG GGKSLCYQIP
ALLLNGLTVV VSPLISLMKD QVDQLQANGV AAACLNSTQT REQQLEVMTG CRTGQIRLLY
IAPERLMLDN FLEHLAHWNP VLLAVDEAHC ISQWGHDFRP EYAALGQLRQ RFPTLPFMAL
TATADDTTRQ DIVRLLGLND PLIQISSFDR PNIRYMLMEK FKPLDQLMRY VQEQRGKSGI
IYCNSRAKVE DTAARLQSKG ISAAAYHAGL ENNVRADVQE KFQRDDLQIV VATVAFGMGI
NKPNVRFVVH FDIPRNIESY YQETGRAGRD GLPAEAMLFY DPADMAWLRR CLEEKPQGQL
QDIERHKLNA MGAFAEAQTC RRLVLLNYFG EGRQEPCGNC DICLDPPKQY DGSTDAQIAL
STIGRVNQRF GMGYVVEVIR GANNQRIRDY GHDKLKVYGM GRDKSHEHWV SVIRQLIHLG
LVTQNIAQHS ALQLTEAARP VLRGESSLQL AVPRIVALKP KAMQKSFGGN YDRKLFAKLR
KLRKSIADES NVPPYVVFND ATLIEMAEQM PITASEMLSV NGVGMRKLER FGKPFMALIR
AHVDGDDEE
