ID   UVRA_RICCN              Reviewed;         955 AA.
AC   Q92G31;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=RC1294;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(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; AE006914; AAL03832.1; -; Genomic_DNA.
DR   PIR; F97861; F97861.
DR   AlphaFoldDB; Q92G31; -.
DR   SMR; Q92G31; -.
DR   EnsemblBacteria; AAL03832; AAL03832; RC1294.
DR   KEGG; rco:RC1294; -.
DR   HOGENOM; CLU_001370_0_2_5; -.
DR   OMA; PFEGIIP; -.
DR   Proteomes; UP000000816; 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; 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..955
FT                   /note="UvrABC system protein A"
FT                   /id="PRO_0000093083"
FT   DOMAIN          322..601
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   DOMAIN          621..951
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   ZN_FING         754..780
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   BINDING         35..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   BINDING         654..661
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   955 AA;  106317 MW;  70ED64A253D7FA68 CRC64;
     MIMNQEYIKV RGAKEHNLKN INVNIPRNKF VVITGLSGSG KSSLAFDTIY AEGQRRYVES
     LSSYARQFLH LQNKPNVESI SGLSPAIAID QKTTSKNPRS TVGTITEIYD YLRLLYARVG
     IPYSPATGLP IHSQTVSEMV DIINELPKGT KIYLLAPIVR GHKGEFKREI MDLKKQGFQK
     LIVNGEVCEI DDLPKLDKNK KHNIEVIVDR IVLDESLGNR LADSLESSLN LAEGITYLEI
     VELPPAVKSE FEKNQRITFS EQYSCPVSGF QLTEIEPRIF SFNSPFGACP KCEGIGKEFF
     FDRDLIVPDQ RIAIKDGAIV PWGSTASKFI LETLKALADH YKFSIEVPFV SLSQNVKDIL
     FEGSGEEAIK FEFHDGSKTQ IIKQPFAGII PSLQEKDRTI ESVLIKEELA KFKSEHKCTA
     CSGFRLKDEA LCVKIANLHI GEVAGMSIAA LQKWFSHLEE KLNKKQLFIA ERILKEITER
     LKFLMNVGLD YLTLSREAGT LSGGESQRIR LASQIGSGLS GVLYVLDEPS IGLHQRDNTR
     LIETLKRLRD LGNTVLVVEH DEETIYEADH IIDIGPGAGI HGGRVIAEGN VEEIKNFEES
     ITGRYLSGRQ TIKVPSETRV GHDNRAIELL GAVSNNLDNV DIKIPLGTFT AITGVSGSGK
     SSLMIHTLYK AALKHLEPTS KVFPGKYREL KGLEYIDKII DINQSPIGRT PRSNPATYTG
     AFTHIRDWFV ELPESKARGY KVGRFSFNVK GGRCEACQGD GLIKIEMHFL PDVYVKCDIC
     NGHRYNRETL EIKYKGKSIA DILMMTVEDA MQFFEKIPLI YEKLITLNEV GLGYIKIGQS
     ATTLSGGEAQ RVKLAKELSR RSTGKTLYIL DEPTTGLHID DINKLLKVLH KLVDMGNTVL
     VIEHNLDVIK TADYIIDVGP EGGDKGGKIV VCGTPADIAA CEESHTGRYL KQYLV