YOAA_ECOLI
ID YOAA_ECOLI Reviewed; 636 AA.
AC P76257; O07973;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Probable ATP-dependent DNA helicase YoaA {ECO:0000305};
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:P27296};
GN Name=yoaA; OrderedLocusNames=b1808, JW1797;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [2]
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 [3]
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 [4]
RP FUNCTION, INTERACTION WITH CHI, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP LYS-51; CYS-168 AND ASP-225.
RX PubMed=26544712; DOI=10.1371/journal.pgen.1005651;
RA Brown L.T., Sutera V.A. Jr., Zhou S., Weitzel C.S., Cheng Y., Lovett S.T.;
RT "Connecting replication and repair: YoaA, a helicase-related protein,
RT promotes azidothymidine tolerance through association with Chi, an
RT accessory clamp loader protein.";
RL PLoS Genet. 11:E1005651-E1005651(2015).
CC -!- FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase (By similarity).
CC Involved in the repair of replication forks and tolerance of the chain-
CC terminating nucleoside analog 3' azidothymidine (AZT). May unwind
CC potentially damaged 3' nascent ends such as those terminated by AZT,
CC promote repair and AZT excision (PubMed:26544712).
CC {ECO:0000250|UniProtKB:P27296, ECO:0000269|PubMed:26544712}.
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:0000250|UniProtKB:P27296};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P27296};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P27296};
CC -!- SUBUNIT: Interacts with the DNA polymerase III subunit Chi (holC).
CC {ECO:0000269|PubMed:26544712}.
CC -!- DISRUPTION PHENOTYPE: Knockout mutants are sensitive to AZT.
CC {ECO:0000269|PubMed:26544712}.
CC -!- SIMILARITY: Belongs to the helicase family. DinG subfamily.
CC {ECO:0000305}.
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DR EMBL; U00096; AAC74878.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15617.1; -; Genomic_DNA.
DR PIR; H64941; H64941.
DR RefSeq; NP_416322.1; NC_000913.3.
DR RefSeq; WP_000128841.1; NZ_LN832404.1.
DR AlphaFoldDB; P76257; -.
DR SMR; P76257; -.
DR BioGRID; 4260341; 111.
DR DIP; DIP-12786N; -.
DR IntAct; P76257; 10.
DR STRING; 511145.b1808; -.
DR PaxDb; P76257; -.
DR PRIDE; P76257; -.
DR EnsemblBacteria; AAC74878; AAC74878; b1808.
DR EnsemblBacteria; BAA15617; BAA15617; BAA15617.
DR GeneID; 946305; -.
DR KEGG; ecj:JW1797; -.
DR KEGG; eco:b1808; -.
DR PATRIC; fig|511145.12.peg.1884; -.
DR EchoBASE; EB3286; -.
DR eggNOG; COG1199; Bacteria.
DR HOGENOM; CLU_012117_2_0_6; -.
DR InParanoid; P76257; -.
DR OMA; KIIVVNH; -.
DR PhylomeDB; P76257; -.
DR BioCyc; EcoCyc:G6992-MON; -.
DR PRO; PR:P76257; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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:0003678; F:DNA helicase activity; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; ISM:EcoCyc.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006301; P:postreplication repair; IMP:EcoCyc.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11472; PTHR11472; 2.
DR Pfam; PF13307; Helicase_C_2; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Iron; Iron-sulfur; Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..636
FT /note="Probable ATP-dependent DNA helicase YoaA"
FT /id="PRO_0000102006"
FT DOMAIN 10..272
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOTIF 225..228
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 45..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 108
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P27296"
FT BINDING 168
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P27296"
FT BINDING 173
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P27296"
FT BINDING 179
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P27296"
FT MUTAGEN 51
FT /note="K->A: Cannot complement the AZT sensitivity of the
FT knockout mutant."
FT /evidence="ECO:0000269|PubMed:26544712"
FT MUTAGEN 168
FT /note="C->A: Cannot complement the AZT sensitivity of the
FT knockout mutant."
FT /evidence="ECO:0000269|PubMed:26544712"
FT MUTAGEN 225
FT /note="D->A: Cannot complement the AZT sensitivity of the
FT knockout mutant."
FT /evidence="ECO:0000269|PubMed:26544712"
SQ SEQUENCE 636 AA; 70378 MW; 14CEBD04CCBE701F CRC64;
MTDDFAPDGQ LAKAIPGFKP REPQRQMAVA VTQAIEKGQP LVVEAGTGTG KTYAYLAPAL
RAKKKVIIST GSKALQDQLY SRDLPTVSKA LKYTGNVALL KGRSNYLCLE RLEQQALAGG
DLPVQILSDV ILLRSWSNQT VDGDISTCVS VAEDSQAWPL VTSTNDNCLG SDCPMYKDCF
VVKARKKAMD ADVVVVNHHL FLADMVVKES GFGELIPEAD VMIFDEAHQL PDIASQYFGQ
SLSSRQLLDL AKDITIAYRT ELKDTQQLQK CADRLAQSAQ DFRLQLGEPG YRGNLRELLA
NPQIQRAFLL LDDTLELCYD VAKLSLGRSA LLDAAFERAT LYRTRLKRLK EINQPGYSYW
YECTSRHFTL ALTPLSVADK FKELMAQKPG SWIFTSATLS VNDDLHHFTS RLGIEQAESL
LLPSPFDYSR QALLCVLRNL PQTNQPGSAR QLAAMLRPII EANNGRCFML CTSHAMMRDL
AEQFRATMTL PVLLQGETSK GQLLQQFVSA GNALLVATSS FWEGVDVRGD TLSLVIIDKL
PFTSPDDPLL KARMEDCRLR GGDPFDEVQL PDAVITLKQG VGRLIRDADD RGVLVICDNR
LVMRPYGATF LASLPPAPRT RDIARAVRFL AIPSSR
