ID   UVRA_PASMU              Reviewed;         943 AA.
AC   P57979;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   03-AUG-2022, entry version 132.
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=PM1951;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(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; AE004439; AAK04035.1; -; Genomic_DNA.
DR   RefSeq; WP_010907420.1; NC_002663.1.
DR   AlphaFoldDB; P57979; -.
DR   SMR; P57979; -.
DR   STRING; 747.DR93_2147; -.
DR   EnsemblBacteria; AAK04035; AAK04035; PM1951.
DR   KEGG; pmu:PM1951; -.
DR   HOGENOM; CLU_001370_0_2_6; -.
DR   OMA; PFEGIIP; -.
DR   Proteomes; UP000000809; 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; 3.30.1490.20; -; 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; Reference proteome;
KW   Repeat; SOS response; Zinc; Zinc-finger.
FT   CHAIN           1..943
FT                   /note="UvrABC system protein A"
FT                   /id="PRO_0000093076"
FT   DOMAIN          310..587
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   DOMAIN          607..937
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   ZN_FING         253..280
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         31..38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   BINDING         640..647
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   943 AA;  104187 MW;  A096DB1162D3C354 CRC64;
     MDKIEVRGAR THNLKNINLT IPRDKLIVIT GLSGSGKSSL AFDTLYAEGQ RRYVESLSAY
     ARQFLSLMEK PDVDHIEGLS PAISIEQKST SHNPRSTVGT VTEIHDYLRL LFARVGEPRC
     PNHDVPLAAQ TISQMVDKVL SLPEESKMML LAPVVKERKG EHVKLLEQIA AQGYIRARID
     GEICDLSDAP KLELHKKHTI EVVVDRFKVR SDLATRLAES FETALELSGG TAVVASMDEP
     ETEELVFSAN FACPHCGYSV PELEPRLFSF NNPAGACPTC DGLGVQQYFD EKRVVQNPSI
     SLASGAVKGW DRRNFYYYQM LTSLAKHYEF DIESPFEALP KKIQQIILNG SGKEEIEFQY
     MNDRGDVVVR HHAFEGILNN MARRYKETES LSVREELAKN ISTCPCHDCG GSRLRQEARH
     VYIGTTTLPD VAEKSIGETL HFFSELHLSG QRAQIAEKIL KEIKERLQFL VNVGLDYLSL
     SRSAETLSGG EAQRIRLASQ IGAGLVGVMY VLDEPSIGLH QRDNERLLNT LLHLRNLGNT
     VIVVEHDEDA IMAADHIIDI GPGAGVHGGQ IVAEGSAKAI MANPHSITGK FLSGVEKIEI
     PAKRTALDKK KMLKLEGATG NNLKSVNLAI PVGLFTCVTG VSGSGKSTLI NDTLFPLAQN
     ALNRAENTQF APYQSISGLE FFDKVIDIDQ SPIGRTPRSN PATYTGLFTP IRELFAGVPE
     SRARGYNPGR FSFNVRGGRC EACQGDGVIK VEMHFLPDVY VPCEQCKGKR YNRETLEIRY
     KGKTIHQVLE MTVEEAREFF DAIPQIARKL QTLMDVGLSY IRLGQSSTTL SGGEAQRVKL
     ATELSKRDTG KTLYVLDEPT TGLHFADIKQ LLTVLHRLRD QGNTIVVIEH NLDVIKTADW
     IIDLGPEGGN GGGQIIATGT PEQVAEVKGS HTARFLKTLL QKR