HELD_ECOLI
ID HELD_ECOLI Reviewed; 684 AA.
AC P15038; P77623;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=DNA helicase IV;
DE EC=3.6.4.12;
DE AltName: Full=75 kDa helicase;
GN Name=helD; OrderedLocusNames=b0962, JW0945;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-27.
RX PubMed=2542273; DOI=10.1016/s0021-9258(18)83182-9;
RA Wood E.R., Matson S.W.;
RT "The molecular cloning of the gene encoding the Escherichia coli 75-kDa
RT helicase and the determination of its nucleotide sequence and gentic map
RT position.";
RL J. Biol. Chem. 264:8297-8303(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
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 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).
CC -!- FUNCTION: Helicase IV catalyzes the unwinding of duplex DNA in the 3'
CC to 5' direction with respect to the bound single strand in a reaction
CC that is dependent upon the hydrolysis of ATP.
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 -!- INTERACTION:
CC P15038; P00936: cyaA; NbExp=3; IntAct=EBI-551473, EBI-1116685;
CC P15038; P0CE47: tufA; NbExp=3; IntAct=EBI-551473, EBI-301077;
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000305}.
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DR EMBL; J04726; AAA23952.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74048.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35727.1; -; Genomic_DNA.
DR PIR; A64837; HJECD4.
DR RefSeq; NP_415482.1; NC_000913.3.
DR RefSeq; WP_001295354.1; NZ_SSZK01000002.1.
DR AlphaFoldDB; P15038; -.
DR SMR; P15038; -.
DR BioGRID; 4263362; 127.
DR BioGRID; 850587; 1.
DR DIP; DIP-9876N; -.
DR IntAct; P15038; 35.
DR STRING; 511145.b0962; -.
DR BindingDB; P15038; -.
DR ChEMBL; CHEMBL4405; -.
DR jPOST; P15038; -.
DR PaxDb; P15038; -.
DR PRIDE; P15038; -.
DR EnsemblBacteria; AAC74048; AAC74048; b0962.
DR EnsemblBacteria; BAA35727; BAA35727; BAA35727.
DR GeneID; 946227; -.
DR KEGG; ecj:JW0945; -.
DR KEGG; eco:b0962; -.
DR PATRIC; fig|1411691.4.peg.1312; -.
DR EchoBASE; EB0421; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_006494_0_1_6; -.
DR InParanoid; P15038; -.
DR OMA; LDFMTIH; -.
DR PhylomeDB; P15038; -.
DR BioCyc; EcoCyc:EG10426-MON; -.
DR BioCyc; MetaCyc:EG10426-MON; -.
DR PRO; PR:P15038; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
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; IPR022161; Helicase_IV_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070; PTHR11070; 2.
DR Pfam; PF12462; Helicase_IV_N; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..684
FT /note="DNA helicase IV"
FT /id="PRO_0000102049"
FT DOMAIN 195..505
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT BINDING 216..223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT BINDING 503
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 70
FT /note="H -> P (in Ref. 1; AAA23952)"
FT /evidence="ECO:0000305"
FT CONFLICT 137..140
FT /note="SALP -> LRVA (in Ref. 1; AAA23952)"
FT /evidence="ECO:0000305"
FT CONFLICT 365..366
FT /note="MH -> ID (in Ref. 1; AAA23952)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 684 AA; 77976 MW; FC1A6250537A4A24 CRC64;
MELKATTLGK RLAQHPYDRA VILNAGIKVS GDRHEYLIPF NQLLAIHCKR GLVWGELEFV
LPDEKVVRLH GTEWGETQRF YHHLDAHWRR WSGEMSEIAS GVLRQQLDLI ATRTGENKWL
TREQTSGVQQ QIRQALSALP LPVNRLEEFD NCREAWRKCQ AWLKDIESAR LQHNQAYTEA
MLTEYADFFR QVESSPLNPA QARAVVNGEH SLLVLAGAGS GKTSVLVARA GWLLARGEAS
PEQILLLAFG RKAAEEMDER IRERLHTEDI TARTFHALAL HIIQQGSKKV PIVSKLENDT
AARHELFIAE WRKQCSEKKA QAKGWRQWLT EEMQWSVPEG NFWDDEKLQR RLASRLDRWV
SLMRMHGGAQ AEMIASAPEE IRDLFSKRIK LMAPLLKAWK GALKAENAVD FSGLIHQAIV
ILEKGRFISP WKHILVDEFQ DISPQRAALL AALRKQNSQT TLFAVGDDWQ AIYRFSGAQM
SLTTAFHENF GEGERCDLDT TYRFNSRIGE VANRFIQQNP GQLKKPLNSL TNGDKKAVTL
LDESQLDALL DKLSGYAKPE ERILILARYH HMRPASLEKA ATRWPKLQID FMTIHASKGQ
QADYVIIVGL QEGSDGFPAA ARESIMEEAL LPPVEDFPDA EERRLMYVAL TRARHRVWAL
FNKENPSPFV EILKNLDVPV ARKP
