UVRA_AQUAE
ID UVRA_AQUAE Reviewed; 926 AA.
AC O66911;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
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}; OrderedLocusNames=aq_686;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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
CC lesions. {ECO:0000255|HAMAP-Rule:MF_00205}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00205}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA family.
CC {ECO:0000255|HAMAP-Rule:MF_00205}.
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DR EMBL; AE000657; AAC06874.1; -; Genomic_DNA.
DR PIR; C70360; C70360.
DR RefSeq; NP_213471.1; NC_000918.1.
DR RefSeq; WP_010880409.1; NC_000918.1.
DR AlphaFoldDB; O66911; -.
DR SMR; O66911; -.
DR STRING; 224324.aq_686; -.
DR PRIDE; O66911; -.
DR EnsemblBacteria; AAC06874; AAC06874; aq_686.
DR KEGG; aae:aq_686; -.
DR PATRIC; fig|224324.8.peg.553; -.
DR eggNOG; COG0178; Bacteria.
DR HOGENOM; CLU_001370_0_2_0; -.
DR InParanoid; O66911; -.
DR OMA; PFEGIIP; -.
DR OrthoDB; 152379at2; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00205; UvrA; 1.
DR InterPro; IPR003593; AAA+_ATPase.
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 Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF17755; UvrA_DNA-bind; 1.
DR Pfam; PF17760; UvrA_inter; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00630; uvra; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA damage; DNA excision; DNA repair; DNA-binding;
KW Excision nuclease; Metal-binding; Nucleotide-binding; Reference proteome;
KW Repeat; SOS response; Zinc; Zinc-finger.
FT CHAIN 1..926
FT /note="UvrABC system protein A"
FT /id="PRO_0000093033"
FT DOMAIN 308..568
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT DOMAIN 588..916
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT ZN_FING 251..278
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT ZN_FING 719..745
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 /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT BINDING 620..627
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
SQ SEQUENCE 926 AA; 103723 MW; F38FA8FA06BAA4F3 CRC64;
MDRIVIRGAR QHNLKNIDVE IPKNKLVVIT GPSGSGKSSL AFDTLYAEGQ RRYVESLSAY
ARQFLGVMEK PEVDSIEGLS PAIAIDQKTT SKNPRSTVGT VTEIYDYLRV LWANVGKPHC
PHCGNLLSGL SAHEILDRIV EKYKGKRVMI LSPIVRGKKG EFRELLRQIE KWGYSRVKVD
GELRRVIEVP PLEKNKKHTI ELVIDRLTVS EEERARLLED VEKALEFSSG LVKIEEVESG
KEELFSEKLV CPEHGFSIPE LSARLFSFNS PYGACPSCKG LGVKWEIDPA VLIDPEKPAV
KAVKIVESGY FNYLRFPIAN VIRKLGYDPR TPWKKLPESV RATVLYGSES LNFEGIIPHL
ERRFLEEESE RIREEIEDYI VEKPCPECKG ARLRKEALAV LIDGKSIWDV VNMPVGKAKE
FFEELYEKLE GKEKIIADRL LKEIIERLGF LVNVGLDYLS LSRSATTLSG GEMQRIRLAT
QLGSKLTGVL YVLDEPSIGL HPRDTSKLIN TLKGLRDLGN TVVVVEHDPE TIESADHVIE
LGPGAGKHGG YLVAQGTVEE IKSHPSSLTG AYLSGRKEIP VPKERRKPSG KFIRIVRAKE
HNLKNINVDI PLGLFVCITG VSGSGKSTLI YDILYKYAKN YFYGTHEQVG EVEKIEGLEN
IDKVINIDQS PIGRTPRSNP ATYTKVFDLI RNLFAQTPEA KARGYKPGRF SFNVKGGRCE
ACQGEGVIKV EMHFLPPVYV TCEVCKGKRY NRETLEITYK GKNIADVLEM TVDEAYDFFE
NHPAIRRKLQ ILKDVGLGYI KLGQPAPTLS GGEAQRIKLA RELSKKETGR TLYLLDEPTT
GLHMDDVKKL IDVLQRLVDK GNTVVVIEHN LDVIKCADWI IDLGPEGGER GGQVVAVGTP
EEVAQNPNSY TGKYLRKYLK KETLKV
