ID UVRA_ECOLI Reviewed; 940 AA.
AC P0A698; P07671; P76788; Q2M6P6;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 27-MAR-2024, entry version 147.
DE RecName: Full=UvrABC system protein A {ECO:0000255|HAMAP-Rule:MF_00205};
DE Short=UvrA protein {ECO:0000255|HAMAP-Rule:MF_00205};
DE AltName: Full=Excinuclease ABC subunit A {ECO:0000255|HAMAP-Rule:MF_00205};
GN Name=uvrA {ECO:0000255|HAMAP-Rule:MF_00205}; Synonyms=dinE;
GN OrderedLocusNames=b4058, JW4019;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3007478; DOI=10.1016/s0021-9258(19)89189-5;
RA Husain I., van Houten B., Thomas D.C., Sancar A.;
RT "Sequences of Escherichia coli uvrA gene and protein reveal two potential
RT ATP binding sites.";
RL J. Biol. Chem. 261:4895-4901(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
RX PubMed=6310514; DOI=10.1093/nar/11.17.5795;
RA Backendorf C., Brandsma J.A., Kartasova T., van de Putte P.;
RT "In vivo regulation of the uvrA gene: role of the '-10' and '-35' promoter
RT regions.";
RL Nucleic Acids Res. 11:5795-5810(1983).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
RX PubMed=6283374; DOI=10.1038/298096a0;
RA Sancar A., Sancar G.B., Rupp W.D., Little J.W., Mount D.W.;
RT "LexA protein inhibits transcription of the E. coli uvrA gene in vitro.";
RL Nature 298:96-98(1982).
RN [7]
RP CHARACTERIZATION.
RX PubMed=1826851; DOI=10.1021/bi00230a005;
RA Myles G.M., Sancar A.;
RT "Isolation and characterization of functional domains of UvrA.";
RL Biochemistry 30:3834-3840(1991).
RN [8]
RP MUTAGENESIS OF CYS-253.
RX PubMed=2550431; DOI=10.1016/s0021-9258(18)71588-3;
RA Navaratnam S., Myles G.M., Strange R.W., Sancar A.;
RT "Evidence from extended X-ray absorption fine structure and site-specific
RT mutagenesis for zinc fingers in UvrA protein of Escherichia coli.";
RL J. Biol. Chem. 264:16067-16071(1989).
RN [9]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 131-250 IN COMPLEX WITH TRCF, AND
RP SUBUNIT.
RX PubMed=22331906; DOI=10.1073/pnas.1115105109;
RA Deaconescu A.M., Sevostyanova A., Artsimovitch I., Grigorieff N.;
RT "Nucleotide excision repair (NER) machinery recruitment by the
RT transcription-repair coupling factor involves unmasking of a conserved
RT intramolecular interface.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:3353-3358(2012).
CC -!- FUNCTION: The UvrABC repair system catalyzes the recognition and
CC processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein.
CC A damage recognition complex composed of 2 UvrA and 2 UvrB subunits
CC scans DNA for abnormalities. When the presence of a lesion has been
CC verified by UvrB, the UvrA molecules dissociate. {ECO:0000255|HAMAP-
CC Rule:MF_00205}.
CC -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for lesions
CC (By similarity). Interacts with TRCF (Mfd). UvrB and TRCF binding to
CC UvrA could be mutually exclusive. {ECO:0000255|HAMAP-Rule:MF_00205,
CC ECO:0000269|PubMed:22331906}.
CC -!- INTERACTION:
CC P0A698; P0AFP2: atl; NbExp=2; IntAct=EBI-552091, EBI-560039;
CC P0A698; P30958: mfd; NbExp=2; IntAct=EBI-552091, EBI-554211;
CC P0A698; P0A698: uvrA; NbExp=2; IntAct=EBI-552091, EBI-552091;
CC P0A698; P0A8F8: uvrB; NbExp=7; IntAct=EBI-552091, EBI-552176;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00205}.
CC -!- MISCELLANEOUS: Binds about 2 zinc atoms/molecule.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA family.
CC {ECO:0000255|HAMAP-Rule:MF_00205}.
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DR EMBL; M13495; AAA24754.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43152.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77028.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78060.1; -; Genomic_DNA.
DR EMBL; X01621; CAA25764.1; -; Genomic_DNA.
DR EMBL; J01721; AAA24753.1; -; Genomic_DNA.
DR PIR; A23869; BVECUA.
DR RefSeq; NP_418482.1; NC_000913.3.
DR RefSeq; WP_000357740.1; NZ_STEB01000022.1.
DR PDB; 4DFC; X-ray; 2.80 A; B/D=131-250.
DR PDBsum; 4DFC; -.
DR AlphaFoldDB; P0A698; -.
DR SMR; P0A698; -.
DR BioGRID; 4262670; 52.
DR BioGRID; 852853; 2.
DR ComplexPortal; CPX-2151; UvrAB DNA damage sensor complex.
DR ComplexPortal; CPX-2155; TRCF-UvrA complex.
DR DIP; DIP-35876N; -.
DR IntAct; P0A698; 17.
DR STRING; 511145.b4058; -.
DR jPOST; P0A698; -.
DR PaxDb; 511145-b4058; -.
DR EnsemblBacteria; AAC77028; AAC77028; b4058.
DR GeneID; 75204201; -.
DR GeneID; 948559; -.
DR KEGG; ecj:JW4019; -.
DR KEGG; eco:b4058; -.
DR PATRIC; fig|1411691.4.peg.2647; -.
DR EchoBASE; EB1054; -.
DR eggNOG; COG0178; Bacteria.
DR HOGENOM; CLU_001370_0_2_6; -.
DR InParanoid; P0A698; -.
DR OMA; EFFKAVP; -.
DR OrthoDB; 9809851at2; -.
DR PhylomeDB; P0A698; -.
DR BioCyc; EcoCyc:EG11061-MONOMER; -.
DR BioCyc; MetaCyc:EG11061-MONOMER; -.
DR BRENDA; 3.6.1.3; 2026.
DR PRO; PR:P0A698; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1990391; C:DNA repair complex; IPI:ComplexPortal.
DR GO; GO:0009380; C:excinuclease repair complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:EcoCyc.
DR GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IMP:EcoCyc.
DR GO; GO:0006289; P:nucleotide-excision repair; NAS:ComplexPortal.
DR GO; GO:0000715; P:nucleotide-excision repair, DNA damage recognition; IDA:ComplexPortal.
DR GO; GO:0006294; P:nucleotide-excision repair, preincision complex assembly; NAS:ComplexPortal.
DR GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR CDD; cd03270; ABC_UvrA_I; 1.
DR CDD; cd03271; ABC_UvrA_II; 1.
DR Gene3D; 1.10.8.280; ABC transporter ATPase domain-like; 1.
DR Gene3D; 1.20.1580.10; ABC transporter ATPase like domain; 2.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_00205; UvrA; 1.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004602; UvrA.
DR InterPro; IPR041552; UvrA_DNA-bd.
DR InterPro; IPR041102; UvrA_inter.
DR NCBIfam; TIGR00630; uvra; 1.
DR PANTHER; PTHR43152; UVRABC SYSTEM PROTEIN A; 1.
DR PANTHER; PTHR43152:SF3; UVRABC SYSTEM PROTEIN A; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF17755; UvrA_DNA-bind; 1.
DR Pfam; PF17760; UvrA_inter; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; DNA damage; DNA excision; DNA repair;
KW DNA-binding; Excision nuclease; Metal-binding; Nucleotide-binding;
KW Reference proteome; Repeat; SOS response; Zinc; Zinc-finger.
FT CHAIN 1..940
FT /note="UvrABC system protein A"
FT /id="PRO_0000093049"
FT DOMAIN 310..587
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT DOMAIN 607..937
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT ZN_FING 253..280
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT ZN_FING 740..766
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 640..647
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MUTAGEN 253
FT /note="C->A,H,S: Reduced activity."
FT /evidence="ECO:0000269|PubMed:2550431"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:4DFC"
FT STRAND 148..160
FT /evidence="ECO:0007829|PDB:4DFC"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:4DFC"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:4DFC"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:4DFC"
FT STRAND 196..207
FT /evidence="ECO:0007829|PDB:4DFC"
FT HELIX 216..227
FT /evidence="ECO:0007829|PDB:4DFC"
FT STRAND 228..238
FT /evidence="ECO:0007829|PDB:4DFC"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:4DFC"
SQ SEQUENCE 940 AA; 103868 MW; D61AAEB6514B860C CRC64;
MDKIEVRGAR THNLKNINLV IPRDKLIVVT GLSGSGKSSL AFDTLYAEGQ RRYVESLSAY
ARQFLSLMEK PDVDHIEGLS PAISIEQKST SHNPRSTVGT ITEIHDYLRL LFARVGEPRC
PDHDVPLAAQ TVSQMVDNVL SQPEGKRLML LAPIIKERKG EHTKTLENLA SQGYIRARID
GEVCDLSDPP KLELQKKHTI EVVVDRFKVR DDLTQRLAES FETALELSGG TAVVADMDDP
KAEELLFSAN FACPICGYSM RELEPRLFSF NNPAGACPTC DGLGVQQYFD PDRVIQNPEL
SLAGGAIRGW DRRNFYYFQM LKSLADHYKF DVEAPWGSLS ANVHKVVLYG SGKENIEFKY
MNDRGDTSIR RHPFEGVLHN MERRYKETES SAVREELAKF ISNRPCASCE GTRLRREARH
VYVENTPLPA ISDMSIGHAM EFFNNLKLAG QRAKIAEKIL KEIGDRLKFL VNVGLNYLTL
SRSAETLSGG EAQRIRLASQ IGAGLVGVMY VLDEPSIGLH QRDNERLLGT LIHLRDLGNT
VIVVEHDEDA IRAADHVIDI GPGAGVHGGE VVAEGPLEAI MAVPESLTGQ YMSGKRKIEV
PKKRVPANPE KVLKLTGARG NNLKDVTLTL PVGLFTCITG VSGSGKSTLI NDTLFPIAQR
QLNGATIAEP APYRDIQGLE HFDKVIDIDQ SPIGRTPRSN PATYTGVFTP VRELFAGVPE
SRARGYTPGR FSFNVRGGRC EACQGDGVIK VEMHFLPDIY VPCDQCKGKR YNRETLEIKY
KGKTIHEVLD MTIEEAREFF DAVPALARKL QTLMDVGLTY IRLGQSATTL SGGEAQRVKL
ARELSKRGTG QTLYILDEPT TGLHFADIQQ LLDVLHKLRD QGNTIVVIEH NLDVIKTADW
IVDLGPEGGS GGGEILVSGT PETVAECEAS HTARFLKPML
//
