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UVRA_PAULE
ID   UVRA_PAULE              Reviewed;         689 AA.
AC   P52087;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 80.
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   Paucimonas lemoignei (Pseudomonas lemoignei).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paucimonas.
OX   NCBI_TaxID=29443;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8269961; DOI=10.1111/j.1432-1033.1993.tb18424.x;
RA   Jendrossek D., Mueller B., Schlegel G.;
RT   "Cloning and characterization of the poly(hydroxyalkanoic acid)-
RT   depolymerase gene locus, phaZ1, of Pseudomonas lemoignei and its gene
RT   product.";
RL   Eur. J. Biochem. 218:701-710(1993).
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; Z22595; CAA80311.1; -; Genomic_DNA.
DR   PIR; S39531; S39531.
DR   AlphaFoldDB; P52087; -.
DR   SMR; P52087; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR041552; UvrA_DNA-bd.
DR   Pfam; PF17755; UvrA_DNA-bind; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 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..>689
FT                   /note="UvrABC system protein A"
FT                   /id="PRO_0000093079"
FT   DOMAIN          211..491
FT                   /note="ABC transporter"
FT   ZN_FING         651..677
FT                   /note="C4-type"
FT   BINDING         48..55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         538..545
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   NON_TER         689
SQ   SEQUENCE   689 AA;  75705 MW;  16591F618E7C67F5 CRC64;
     MRKKTDLHSH GTSEKQIEGF VQVRGAREHN LKDVHLDIPR NALVVFTGIS GSGKSSLAFG
     TLYAEAQRRY LESVSPYARR LFHQMSVPEV DSIEGLPPAI ALQQQRGAPT TRSSVGSITT
     LSNSLRMLYS RAGNYPKGQD ILYAESFSPN TPEGACPTCH GLGRVYEVTE QSMVPDDSKT
     IRERAIAAWP PAWHGQNLRD ILTTLGYDID IPWRDLPKKD RKWILFTEEQ PVVPVYAGFT
     LDEVRHALKR KETPSYQGTF TSARKYVLDT FANTESPAMK KRVSQYMVGK ECTLCQGKRL
     RPESLAVTFA GYDITELSRL PLKHLATLLH PYAQENTPDW DKLAAKNPEK AIVTQRIAED
     LSNRLSVLLS LGLGYLTLER STPTLSPGEL QRLRLATQVH SNLFGVVYVL DEPSAGLHPA
     DTQALLAALD RLKQAGNSLF VVEHALGVIR HADWIVDVGP EAGEHGGRIL YSGPPQGLSE
     VAESHTRRYL FPDKEADIFA KQPSRSPQGW LQVAGVTRNN LDNLTAAFPL GVLTSVSGVS
     GSGKSSLVSQ VLVELVSKAL GQELVAEAEQ GESIEHDTPA TLGGRITAGM ESIKRLVTVD
     QKPIGRTPRS NLATYTGLFD HVRKLFASTR AAKARHYDAG RFSFNVAKGR CGNCEGEGFV
     MVELLFLPSV YAPCPVCKGT RFNAKTLEI
 
 
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