ID   UVRA_VITST              Reviewed;         569 AA.
AC   Q08518;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=UvrABC system protein A;
DE            Short=UvrA protein;
DE   AltName: Full=Excinuclease ABC subunit A;
DE   Flags: Fragment;
GN   Name=uvrA;
OS   Vitreoscilla stercoraria.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Vitreoscilla.
OX   NCBI_TaxID=61;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C1;
RX   PubMed=7765771; DOI=10.1007/bf00902733;
RA   Liu S.C., Liu Y.X., Webster D.A., Stark B.C.;
RT   "Sequence of the region downstream of the Vitreoscilla hemoglobin gene: vgb
RT   is not part of a multigene operon.";
RL   Appl. Microbiol. Biotechnol. 42:304-308(1994).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for
CC       lesions. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA family.
CC       {ECO:0000305}.
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DR   EMBL; L21670; AAA75507.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q08518; -.
DR   SMR; Q08518; -.
DR   PRIDE; Q08518; -.
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-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004602; UvrA.
DR   Pfam; PF00005; ABC_tran; 1.
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..569
FT                   /note="UvrABC system protein A"
FT                   /id="PRO_0000093115"
FT   DOMAIN          223..550
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   ZN_FING         359..385
FT                   /note="C4-type"
FT   BINDING         259..266
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   NON_TER         1
SQ   SEQUENCE   569 AA;  61918 MW;  97D7E94D4851BA1F CRC64;
     ARAIRVHGKL EPIYVETVAE LPEASRLYTV RARCERSPLC VCRWRKFHHI SAWPLSKTLD
     FFQNLDLGGN KQQIAEKVLK EITERLGFLI NVGLNYLSLA RSAETLSGGE AQRIRLASQI
     GSGLTGVMYV LDEPSIGLHQ RDNDRLLGTL KHLRDLGNSV IVVEHDEDAI RAADYVVDMG
     PGAGELGGAV LIADTPEKIA ACEQSITGRY LSGKEAIYIP AQRTPKDAER MLVLKGASGQ
     NLKDVTLELP LGLMTCITGV SGSGKSTLIN DTLAKIAQRD LNRATKDEPS PYTEIQGLEQ
     LDKVINVDQS PIGRTPRSNP ATYTGVFTPI RELFAGVPVS RERGYNVGRF SFNVKGGRCE
     ACQGDGVLKV EMHFLPDVYV PCEVCHGKRY NRETLEILYK GKNIHQVLEM TVAEAHAFFE
     AVPTLSRKLQ TLMDVGLSYV RLGQSATTLS GGEAQRVKLA LELSKRDTGR TLYILDEPTT
     GLHFADIALL LEVITRLKGK GNSIVIIEHN LDVIKTADYI IDLGPEGGDG DGGGRIIAQG
     TPEDVAATAG SYTGQYLSQV LANSQTAAV