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