ID   UVRA_XANCP              Reviewed;         988 AA.
AC   Q8PBH3;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 117.
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}; Synonyms=uvrA1;
GN   OrderedLocusNames=XCC1148;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(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; AE008922; AAM40447.1; -; Genomic_DNA.
DR   RefSeq; NP_636523.1; NC_003902.1.
DR   RefSeq; WP_011036348.1; NC_003902.1.
DR   AlphaFoldDB; Q8PBH3; -.
DR   SMR; Q8PBH3; -.
DR   STRING; 340.xcc-b100_3190; -.
DR   EnsemblBacteria; AAM40447; AAM40447; XCC1148.
DR   KEGG; xcc:XCC1148; -.
DR   PATRIC; fig|190485.4.peg.1228; -.
DR   eggNOG; COG0178; Bacteria.
DR   HOGENOM; CLU_001370_0_2_6; -.
DR   OMA; PFEGIIP; -.
DR   Proteomes; UP000001010; 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; 3.40.50.300; -; 3.
DR   HAMAP; MF_00205; UvrA; 1.
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   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   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..988
FT                   /note="UvrABC system protein A"
FT                   /id="PRO_0000093117"
FT   DOMAIN          312..589
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   DOMAIN          609..938
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   ZN_FING         255..282
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   ZN_FING         741..767
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   REGION          948..988
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        960..976
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         33..40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   BINDING         642..649
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   988 AA;  109376 MW;  9CDA27E6E5832825 CRC64;
     MAMDFIRIRG ARTHNLKNID LDLPRDKLIV ITGLSGSGKS SLAFDTIYAE GQRRYVESLS
     AYARQFLSVM EKPDLDHIEG LSPAISIEQK STSHNPRSTV GTITEIYDYL RLLYARVGQP
     RCPDHGFPLE AQTVSQMVDH MLTLDPEQRY MLLAPVIRDR KGEHAQVFEQ LRAQGFVRVR
     VDGELYEIDA VPPLALRQKH TIEAVIDRFR PREDIKQRLA ESFETALKLG EGMVAVQSLD
     DATAAPHLFS SKYSCPVCDY SLPELEPRLF SFNAPVGACP SCDGLGVAEF FDPDRVVVHP
     ELSLSAGAVR GWDRRNAYYF QLIASLAKHY KFDVDAVWNT LPAKVRQAVL FGSGDEVISF
     TYFTDAGGRT TRKHRFEGIL PNLERRYRET ESPAVREELT KYVSQQPCPA CNGTRLNRAA
     RNVFVADRPL PELVVLPVNE ALNFFRGLSL PGWRGEIASK IVKEIGERLG FLVDVGLDYL
     TLERKADTLS GGEAQRIRLA SQIGAGLVGV MYVLDEPSIG LHQRDNERLL GTLTRLRDLG
     NTVIVVEHDE DAIRLADHVL DIGPGAGVHG GEICAQGTLQ DILESPRSLT GQYLSGKRRI
     EIPKQRHKPN PKMMLHLRGA TGNNLKNVDL EIPAGLLTCI TGVSGSGKST LINDTLFTLA
     ANEINGASHT VAPHREVENL DLFDKVVDID QSPIGRTPRS NPATYTGMFT PLRELFAQVP
     ESRARGYSPG RFSFNVRGGR CEACQGDGMI KVEMHFLPDV YVPCDVCHGK RYNRETLEIR
     YKGFNISDVL QMTVEDALRL FEPVPSIARK LETLVDVGLS YIKLGQSATT LSGGEAQRVK
     LSKELSRRDT GRTLYILDEP TTGLHFHDIE ALLGVLHKLR DEGNTVVVIE HNLDVIKTAD
     WIVDLGPEGG HRGGTILVSG TPEDVAAHKA SYTGQFLAKM LPSVKARETR PAAMANKPDA
     RPPRKVKPEK VAKATKTATK KTAKKKAS