UVRA_STRPN
ID UVRA_STRPN Reviewed; 943 AA.
AC P63384; Q97SX7;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=SP_0186;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
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; AE005672; AAK74367.1; -; Genomic_DNA.
DR PIR; F95021; F95021.
DR RefSeq; WP_001152899.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; P63384; -.
DR SMR; P63384; -.
DR STRING; 170187.SP_0186; -.
DR EnsemblBacteria; AAK74367; AAK74367; SP_0186.
DR GeneID; 60233172; -.
DR KEGG; spn:SP_0186; -.
DR eggNOG; COG0178; Bacteria.
DR OMA; PFEGIIP; -.
DR PhylomeDB; P63384; -.
DR BioCyc; SPNE170187:G1FZB-194-MON; -.
DR Proteomes; UP000000585; 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; Repeat; SOS response;
KW Zinc; Zinc-finger.
FT CHAIN 1..943
FT /note="UvrABC system protein A"
FT /id="PRO_0000093100"
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; 104185 MW; B1E0A86DC48ED424 CRC64;
MQDKIVIHGA RAHNLKNIDV EIPRDKLVVV TGLSGSGKSS LAFDTLYAEG QRRYVESLSA
YARQFLGNME KPDVDAIDGL SPAISIDQKT TSKNPRSTVG TTTEINDYLR LLYARVGTPY
CINGHGAINA SSVEQIVDKV LELPERQRLQ ILAPVIRKKK GQHKSVIEKV QKDGYVRVRV
DGEVYDVTEV PELSKSKQHN IDVVVDRIVI KEGIRSRLFD SIEAALRIAE GYVIIDTMDD
SELLFSEHYA CPVCGFTVPE LEPRLFSFNA PFGSCSECDG LGIKLEVDTD LVVPDASKTL
REGALAPWNP ISSNYYPNML EQAMKVFGVA MDKPFEDLSE EDKNLILYGS DGKEFHFHYE
NEFGGVRDID IPFEGVINNI KRRYHETNSD YTRTQMRLYM NELTCGTCQG YRLNDQALSV
RVGGQQGPHI GEISDLSIAD HLDLVSQLTL SENEAIIARP ILKEIKDRLT FLNNVGLNYL
TLSRSAGTLS GGESQRIRLA TQIGSNLSGV LYILDEPSIG LHQRDNDRLI ASLKKMRDLG
NTLIVVEHDE DTMREADYLI DVGPGAGVFG GEIVAAGTPK QVARNSKSIT GQYLSGKRVI
PVPEERRVGN GRFIEVIGAR ENNLQNVTAR FPLGKFIAVT GVSGSGKSTL INSILKKAIA
QKLNRNSDKP GKFKTITGIE HVDRLIDIDQ SPIGRTPRSN PATYTGVFDD IRDLFAQTNE
AKIRGYKKGR FSFNVKGGRC EACSGDGIIK IEMHFLPDVY VACEVCHGTR YNSETLEVHY
KEKNISQVLD MTVNDAVEFF QHIPKIQRKL QTIKDVGLGY VTLGQPATTL SGGEAQRMKL
ASELHKRSTG KSFYILDEPT TGLHTEDIAR LLKVLARFVD DGNTVLVIEH NLDVIKTADH
IIDLGPEGGV GGGTIIVTGT PEEVAANEAS YTGHYLKGKL HHE
