ID   UVRA_NEIGO              Reviewed;         950 AA.
AC   Q50968;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 103.
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};
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9197406; DOI=10.1007/pl00008608;
RA   Black C.G., Fyfe J.A.M., Davies J.K.;
RT   "Cloning, nucleotide sequence and transcriptional analysis of the uvrA gene
RT   from Neisseria gonorrhoeae.";
RL   Mol. Gen. Genet. 254:479-485(1997).
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; U34760; AAA84885.1; -; Genomic_DNA.
DR   RefSeq; WP_003692252.1; NZ_QNRU01000012.1.
DR   AlphaFoldDB; Q50968; -.
DR   SMR; Q50968; -.
DR   PATRIC; fig|485.41.peg.2376; -.
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; 3.30.1490.20; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_00205; UvrA; 1.
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; 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; Repeat; SOS response;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..950
FT                   /note="UvrABC system protein A"
FT                   /id="PRO_0000093071"
FT   DOMAIN          319..596
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   DOMAIN          616..945
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   ZN_FING         262..289
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   ZN_FING         748..774
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   BINDING         42..49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   BINDING         649..656
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   950 AA;  105552 MW;  359806240AADD6F1 CRC64;
     MCNHHPRHSH DNDTIRIRGA RTHNLKNIDL DIPRHKLVVV TGLSGSGKSS LAFDTLYAEG
     QRRYVESLSA YARQFLQMMD KPDVDLIEGL SPAISIEQKS TSHNPRSTVG TVTEIHDYLR
     LLYARVGTPY CPEHNLSLSS QTVSQMVDAV LKLPEDTRVM ILGPAVRERK GEFVDFFADL
     QAQGFARVRV DGEVYQLDEV PKLEKNIKHN IDVVIDRVKV KADIKQRLAE SFETALRHGN
     ERALAMEMDS GEEHWFSARF ACPVCSYSLP ELEPRLFSFN NPMGSCPTCD GLGNTNFFDP
     EKVVAHPELS LATGAIDGWD KRNQFYFQMI QSLAHHYKFD VNVAWETLPE KVKKVVLHGS
     GKEVIDFTYL SERGTTFNRS HAFEGIIPNL ERRYRETDSE TVREKLREYQ NHRACPSCGG
     ARLRKEARYV YVGGEPLHEV SAWPLTKTHR FFETLDLDGN KKQIAEKILK EITERLGFLI
     NVGLDYLNLS RSAETLSGGE AQRIRLASQI GSGLTGVMYV LDEPSIGLHQ RDNDRLLATL
     KRLRDLGNSV IVVEHDEDAI READFVVDMG PGAGEHGGNV LIADTPENVA KCEKSVTGQY
     LGGKKSIAVP SERTPVNPGR MLVLKGARGN NLKNVTLELP LGLITCITGV SGSGKSTLIN
     DTLAKITARE LNRAQEEPAP YDDIRGLEHL DKVINVDQSP IGRTPRSNPA TYTGLFTPIR
     ELFAGVPLSR ERGYNVGRFS FNVKGGRCEA CQGDGVIKVE MHFLPDVYVP CEVCHGKRYN
     RETLEIQYKG KNISQVLDMT VEEAREFFDA VPTVSRKLQT LMDVGLGYIR LGQSATTLSG
     GEAQRVKLAL ELSKRDTGRT LYILDEPTTG LHFADIALLL EVIGRLKGKG NSIVIIEHNL
     DVIKTADWIV DLGPEGGDGG GKVIAKGSPE QVAKIKGSYT GKYLKVALNK