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UVRA_VIBCH
ID   UVRA_VIBCH              Reviewed;         940 AA.
AC   Q9KUW5;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 119.
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=VC_0394;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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; AE003852; AAF93567.1; -; Genomic_DNA.
DR   PIR; A82329; A82329.
DR   RefSeq; NP_230048.1; NC_002505.1.
DR   RefSeq; WP_000357696.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KUW5; -.
DR   SMR; Q9KUW5; -.
DR   STRING; 243277.VC_0394; -.
DR   PRIDE; Q9KUW5; -.
DR   DNASU; 2614991; -.
DR   EnsemblBacteria; AAF93567; AAF93567; VC_0394.
DR   GeneID; 57739133; -.
DR   KEGG; vch:VC_0394; -.
DR   PATRIC; fig|243277.26.peg.369; -.
DR   eggNOG; COG0178; Bacteria.
DR   HOGENOM; CLU_001370_0_2_6; -.
DR   OMA; PFEGIIP; -.
DR   BioCyc; VCHO:VC0394-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
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; 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; 2.
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..940
FT                   /note="UvrABC system protein A"
FT                   /id="PRO_0000093111"
FT   DOMAIN          309..586
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   DOMAIN          606..936
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   ZN_FING         252..279
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   ZN_FING         739..765
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   BINDING         31..38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   BINDING         639..646
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   940 AA;  104328 MW;  84F93B9DF686F6F2 CRC64;
     MDKIEVRGAR THNLKNINLT IPRDKLIVIT GLSGSGKSSL AFDTLYAEGQ RRYVESLSAY
     ARQFLSLMEK PDVDHIEGLS PAISIEQKST SHNPRSTVGT ITEVYDYLRL LYARVGEPRC
     PEHQVPLKAQ TISQMVDKVL ELPEGSKMML LATIVKERKG EHVKTLENLA AQGFIRARID
     GETCDLTDPP KLELHKKHTI EVIVDRFKVR SDLQQRLAES FETALELSGG IVVVAPMEGD
     GEEQIFSANF ACPHCGYSMR ELEPRLFSFN NPAGACPTCD GLGVQQYFDP DRVIQDANLS
     LAQGAIRGWD QKNFYYFQML TALAEHYDFD VHTPFNKLSK KIQEIILHGS GRTEIEFKYI
     NDRGDIRLKK HPFEGILHNL ERRYRDTESN SVREELAKYI SNKPCSSCDG TRLKIEARNV
     FINDTALPTI VELSIADALT FFQELKLEGQ RAQIAEKVMK EINDRLQFLV NVGLNYLNLS
     RSAETLSGGE AQRIRLASQI GAGLVGVMYV LDEPSIGLHQ RDNERLLQTL THLRNLGNTV
     LVVEHDEDAI RMADHVIDIG PGAGVHGGMV VAEGNVEEII ANPNSLTGQY LSGVKKIAVP
     EQRTPKDAKK TVELKGAVGN NLKNVDLSIP VGLFTCVTGV SGSGKSTLIN DTFFKIAHTA
     LNGATTATPA PYRSIQGLEH FDKVIDIDQS PIGRTPRSNP ATYTGIFTPI RELFAGTQES
     RSRGYQPGRF SFNVRGGRCE ACQGDGVIKV EMHFLPDVYV PCDVCKGKRY NRETLEVRYK
     GKTIDEVLDM TVEDAREFFD PVPVIARKLQ TLMDVGLSYI RLGQSATTLS GGEAQRVKLA
     RELSKRDTGK TLYILDEPTT GLHFHDIQQL LSVLHRLRDH GNTVVVIEHN LDVIKTADWI
     IDLGPEGGQG GGLIIAEGTP EDVAQIEASH TARFLKPLLN
 
 
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