UVRA_STRP8
ID UVRA_STRP8 Reviewed; 942 AA.
AC Q8NZJ2;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=spyM18_1890;
OS Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=186103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS8232;
RX PubMed=11917108; DOI=10.1073/pnas.062526099;
RA Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D.,
RA Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A.,
RA Veasy L.G., Musser J.M.;
RT "Genome sequence and comparative microarray analysis of serotype M18 group
RT A Streptococcus strains associated with acute rheumatic fever outbreaks.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
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; AE009949; AAL98394.1; -; Genomic_DNA.
DR RefSeq; WP_011018187.1; NC_003485.1.
DR AlphaFoldDB; Q8NZJ2; -.
DR SMR; Q8NZJ2; -.
DR KEGG; spm:spyM18_1890; -.
DR HOGENOM; CLU_001370_2_1_9; -.
DR OMA; PFEGIIP; -.
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:0022857; F:transmembrane transporter activity; IEA:UniProt.
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; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00630; uvra; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA damage; DNA excision; DNA repair; DNA-binding;
KW Excision nuclease; Metal-binding; Nucleotide-binding; Repeat; SOS response;
KW Zinc; Zinc-finger.
FT CHAIN 1..942
FT /note="UvrABC system protein A"
FT /id="PRO_0000093105"
FT DOMAIN 308..589
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT DOMAIN 609..937
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 740..766
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT BINDING 641..648
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
SQ SEQUENCE 942 AA; 104048 MW; 471CF488AE9E2554 CRC64;
MQNKIIIHGA RAHNLKNIDV EIPRDKLVIV TGLSGSGKSS LAFDTIYAEG QRRYVESLSA
YARQFLGNME KPDVDSIDGL SPAISIDQKT TSKNPRSTVG TVTEINDYLR LLYARVGTPY
CINGHGAITA SSAEQIVEQV LALPERTRMQ ILAPIVRRKK GQHKTIFEKI QKDGYVRVRV
DGDIFDVTEV PELSKSKMHN IEVVIDRLVN KDGIRSRLFD SVEAALRLGD GYLMIDTMDG
NELLFSEHYS CPVCGFTVPE LEPRLFSFNA PFGSCPTCDG LGIKLEVDLD LVVPDPSKSL
KEGALAPWNP ISSNYYPTML EQAMASFGVD MDTPFEALTE EERDLVLYGS GDREFHFHYV
NDFGGERNID IPFEGVVTNV NRRYHETNSD YTRNVMRGYM NELTCATCHG YRLNDQALCV
HVGGEEGPHI GQISELSIAD HLQLLEELEL TENESTIAKP IVKEIHDRLT FLNNVGLNYL
TLSRAAGTLS GGESQRIRLA TQIGSNLSGV LYILDEPSIG LHQRDNDRLI ESLKKMRDLG
NTLIVVEHDE DTMMQADWLI DVGPGAGEFG GEIIASGTPK QVAKNKKSIT GQYLSGKKFI
PVPLERRSGN GRFIEIKGAA QNNLQSLDVR FPLGKFIAVT GVSGSGKSTL VNSILKKAVA
QKLNRNADKP GKYHSISGIE HIERLIDIDQ SPIGRTPRSN PATYTGVFDD IRDLFAQTNE
AKIRGYKKGR FSFNVKGGRC EACSGDGIIK IEMHFLPDVY VPCEVCHGRR YNSETLEVHY
KEKNIAEVLD MTVDDALVFF SAIPKIARKI QTIKDVGLGY VTLGQPATTL SGGEAQRMKL
ASELHKRSTG KSLYILDEPT TGLHTDDIAR LLKVLERFVD DGNTVLVIEH NLDVIKSADH
IIDLGPEGGV GGGQIVATGT PEEVAQVKES YTGHYLKVKL QQ
