ID   UVRA_MICLU              Reviewed;         992 AA.
AC   P13567;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 115.
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   Micrococcus luteus (Micrococcus lysodeikticus).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Micrococcus.
OX   NCBI_TaxID=1270;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2549377; DOI=10.1007/bf02464901;
RA   Shiota S., Nakayama H.;
RT   "Micrococcus luteus homolog of the Escherichia coli uvrA gene:
RT   identification of a mutation in the UV-sensitive mutant DB7.";
RL   Mol. Gen. Genet. 217:332-340(1989).
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; X15867; CAA33877.1; -; Genomic_DNA.
DR   PIR; S04781; S04781.
DR   AlphaFoldDB; P13567; -.
DR   SMR; P13567; -.
DR   STRING; 1232675.GCA_000309825_01852; -.
DR   PRIDE; P13567; -.
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; IPR003593; AAA+_ATPase.
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   SMART; SM00382; AAA; 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..992
FT                   /note="UvrABC system protein A"
FT                   /id="PRO_0000093063"
FT   DOMAIN          360..639
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   DOMAIN          659..988
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   ZN_FING         302..330
FT                   /note="C4-type; atypical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   ZN_FING         791..817
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         62..69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   BINDING         692..699
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
SQ   SEQUENCE   992 AA;  108692 MW;  C3976AF491A28BBE CRC64;
     MPKNSSTTVS SAVEAHAGGL ASGPGGARSG ERDRIVVQGA REHNLKDVDV SFPRDAMVVF
     TGLSGSGKSS LAFDTIFAEG QRRYVESLSS YARMFLGRVD KPDVDFIEGL SPAVSIDQKS
     TNRNPRSTVG TITEIYDYMR LLWARVGVPH CPQCGEPVSR QTPQQIVDQL EELPERTRFQ
     VLAPVVRGRK GEFVDLFRDL STQGFAVVDG ETVQLSDPPV LKKQVKHTIA VVVDRLAMKE
     GIRQRLTDSV ETALKLADGL VVAEFVDVEP VAEKGKKNTA EFGGRDAEGN PRYRSFSEKL
     SCPNGHEQTV DEIEPRSFSF NNPFGACPEC TGIGSRLQVD PDLVVANDEL SLREGAVVPW
     SLGKSTSDYW LRVLGGLGKE MGFSLDTPWK DLTEAERDAV LHGKDFKVEV TFRNRFGRER
     RYTTGFEGVI PYVMRKHGET ESDGARERYE SFMREIPCPA CHGARLNPTV LNVLVGGLSI
     ADATRLPMRE AMEFFSGLRL TDRERQIADQ VLKEILARLA FLLDVGLEYL NLERPAGTLS
     GGEAQRIRLA TQIGSGLVGV LYVLDEPSIG LHQRDNRRLI ETLLRLRDLG NTLIVVEHDE
     DTIAEADWIV DIGPRAGEYG GEVVHSGSLA DLKANTRSVT GDYLSGRRSI AVPERRRVPE
     KGRVLTVRGA QENNLKDVSV QVPLGVLTAV TGVSGSGKST LINEILYKVL ANRLNGAKLV
     PGRHRSVEGL EHLDKVVHVD QSPIGRTPRS NPATYTGVFD AIRKLFAETP EAKVRGYQQG
     RFSFNIKGGR CEACAGDGTL KIEMNFLPDV YVPCEVCHGA RYNRETLEVT YKGKNIAEVL
     DMPIEEAADF FSAYTRISRY LDTLVDVGLG YVRLGQPATT LSGGEAQRVK LAAELQKRSN
     GRTIYVLDEP TTGLHFDDIR KLLHVLQSLV DKGNTVLTIE HNLDVIKSAD HVIDLGPEGG
     SGGGTIVATG TPEEVARAAE SHTGRFLAEL LA