UVRA_STRMU
ID UVRA_STRMU Reviewed; 943 AA.
AC P72481;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 141.
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=SMU_1851;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 469-604.
RC STRAIN=GS-5;
RA Peruzzi F., Piggot P.J., Daneo-Moore L.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
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; AE014133; AAN59473.1; -; Genomic_DNA.
DR EMBL; U75479; AAB41197.1; -; Genomic_DNA.
DR RefSeq; NP_722167.1; NC_004350.2.
DR RefSeq; WP_002262666.1; NC_004350.2.
DR AlphaFoldDB; P72481; -.
DR SMR; P72481; -.
DR STRING; 210007.SMU_1851; -.
DR PRIDE; P72481; -.
DR EnsemblBacteria; AAN59473; AAN59473; SMU_1851.
DR KEGG; smu:SMU_1851; -.
DR PATRIC; fig|210007.7.peg.1653; -.
DR eggNOG; COG0178; Bacteria.
DR HOGENOM; CLU_001370_0_2_9; -.
DR OMA; PFEGIIP; -.
DR PhylomeDB; P72481; -.
DR Proteomes; UP000002512; 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: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; 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..943
FT /note="UvrABC system protein A"
FT /id="PRO_0000093099"
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 943 AA; 104119 MW; 8DB3B8F588BB6212 CRC64;
MQDKLIIRGA RAHNLKNIDV EIPRDKLIVM TGLSGSGKSS LAFDTIYAEG QRRYVESLSA
YARQFLGNMD KPDVDSIDGL SPAISIDQKT TSKNPRSTVG TVTEINDYLR LLYARVGIPY
CKNGHGAITA SSVEQIVDQV LILPERTRMQ ILAPVVRRKK GQHKAVFDRI QKDGYVRVRI
DGDIMDVAEV PELSKNKMHN IEVVVDRLVQ KDGIRGRLFD SIEAALHLGD GYVIIDTMDD
HELIFSEHYS CPVCGFTVPE LEPRLFSFNA PFGSCPTCDG LGIKLEVDLD LVIPDENKTL
REGTLAPWNP ISSNYYPQLL EQAMNAFGVD MDKPWKDLSD EDKKLVLHGS GDTAFHFHYQ
NDFGGVRDID IPFEGIISNI SRRYHETNSD FTRNVMRSYM NELPCATCHG YRLNDQALSV
RVGGKEGLNI GQVSELSIAD HLSLLTHLEL SENEKTIATP IVKEIKDRLT FLNNVGLNYL
TLSRSAGTLS GGESQRIRLA TQIGSNLSGV LYILDEPSIG LHQRDNDRLI SSLKKMRDLG
NTLIVVEHDE DTMMAADWLV DVGPGAGALG GEIVASGTPR QVAKNKKSIT GQYLSGKKKI
PVPLDRRKGS GRFIEIKGAA ENNLQNINVK FPLGKFIAVT GVSGSGKSTL VNSILKKVIA
QKLNRNSEKP GKYKSISGIE HIDRLIDIDQ SPIGRTPRSN PATYTGVFDD IRDLFAQTNE
AKIRGYKKGR FSFNVKGGRC EACSGDGIIK IEMHFLPDVY VPCEVCHGTR YNSETLEVHY
KDKNIAEILN MTVNDAAEFF APIPKIARKI RTIKDVGLGY VTLGQPATTL SGGEAQRMKL
ASELHKRSTG KSFYILDEPT TGLHTDDIAR LLKVLERFVD DGNTVLVIEH NLDVIKTADH
IIDLGPEGGV GGGQVIATGT PEQVAEMTES YTGQYLKGRL NEK
