UVRA_RICBR
ID UVRA_RICBR Reviewed; 953 AA.
AC Q1RK71;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=RBE_0162;
OS Rickettsia bellii (strain RML369-C).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=336407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RML369-C;
RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA Fournier P.-E., Claverie J.-M., Raoult D.;
RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT gene exchanges between intracellular pathogens.";
RL PLoS Genet. 2:733-744(2006).
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; CP000087; ABE04243.1; -; Genomic_DNA.
DR RefSeq; WP_011476857.1; NC_007940.1.
DR AlphaFoldDB; Q1RK71; -.
DR SMR; Q1RK71; -.
DR STRING; 336407.RBE_0162; -.
DR PRIDE; Q1RK71; -.
DR EnsemblBacteria; ABE04243; ABE04243; RBE_0162.
DR KEGG; rbe:RBE_0162; -.
DR eggNOG; COG0178; Bacteria.
DR HOGENOM; CLU_001370_0_2_5; -.
DR OMA; PFEGIIP; -.
DR OrthoDB; 152379at2; -.
DR Proteomes; UP000001951; 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; 3.40.50.300; -; 3.
DR HAMAP; MF_00205; UvrA; 1.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
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; 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; Repeat; SOS response;
KW Zinc; Zinc-finger.
FT CHAIN 1..953
FT /note="UvrABC system protein A"
FT /id="PRO_0000278041"
FT DOMAIN 320..599
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT DOMAIN 619..949
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT ZN_FING 752..778
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT BINDING 652..659
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
SQ SEQUENCE 953 AA; 106285 MW; 8D7BF227C2EB5448 CRC64;
MNQEYIKVRG AKEHNLKNIN VDIPRNKFVV ITGLSGSGKS SLAFDTIYAE GQRRYVESLS
SYARQFLHLQ NKPNVESISG LSPAIAIDQK TTSKNPRSTV GTITEIYDYL RLLYARVGIP
YSPATGLPIH SQTVSEMVDI INELPQGTKI YLLAPIVRGH KGEFKREIMN LKKQGFQKLI
VNGETCEIDD LPKLDKNKKH NIEVIVDRIV LDENLGNRLA DSLESSLNLA DGITYLEIVE
LPTAANTEYE KNQRITFSEK YSCPVSGFQL TEIEPRIFSF NSPFGACPKC EGIGKEFFFD
RDLIVPDHRI SIKDGAIVPW GSTSSKFILE TLKALAEHYR FSIESPFSAL SDNIKTILFE
GSGEEAIRFE FHDGSKTQVI HQPFAGIIPS LQEKDRTIES VLIKEELAKF KSEHKCTACN
GYRLKDEALC VKIVNIHIGE VADMSIATLQ QWFAHLEQKL NKKQLFIAER ILKEINERLK
FLMNVGLDYL TLSRESGTLS GGESQRIRLA SQIGSGLSGV LYVLDEPSIG LHQRDNTRLI
ETLKRLRDLG NTVLVVEHDE ETMYEADHII DIGPGAGIHG GRVIAEGNAE EIKNFEESIT
GRYLSGRQTI KVPTQTRTGH DNRAIELIGA VSNNLDNVDI KIPLGTFTAI TGVSGSGKSS
LMIHTLYKAA LKHLEPTAKV FPGKYQKLKG LEYIDKIIDI NQSPIGRTPR SNPATYTGAF
THIRDWFVEL PESKARGYKV GRFSFNVKGG RCEACQGDGL IKIEMHFLPD VYVKCDICNG
HRYNRETLEI KYKGKSIADI LMMTVEDAMQ FFEKIPLIYE KLITLNEVGL GYIKIGQSAT
TLSGGEAQRV KLAKELSRRS TGKTLYILDE PTTGLHIDDI NKLLKVLHKL VDMGNTVLVI
EHNLDVIKTA DYIIDVGPEG GDKGGKIVVH GTPADIAACS ESHTGRYLKQ YLK