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Database: UniProt
Entry: C0R3W1_WOLWR
LinkDB: C0R3W1_WOLWR
Original site: C0R3W1_WOLWR 
ID   C0R3W1_WOLWR            Unreviewed;       931 AA.
AC   C0R3W1;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=UvrABC system protein A {ECO:0000256|ARBA:ARBA00039316, ECO:0000256|HAMAP-Rule:MF_00205};
DE            Short=UvrA protein {ECO:0000256|HAMAP-Rule:MF_00205};
DE   AltName: Full=Excinuclease ABC subunit A {ECO:0000256|ARBA:ARBA00042156, ECO:0000256|HAMAP-Rule:MF_00205};
GN   Name=uvrA {ECO:0000256|HAMAP-Rule:MF_00205,
GN   ECO:0000313|EMBL:ACN95603.1};
GN   OrderedLocusNames=WRi_008740 {ECO:0000313|EMBL:ACN95603.1};
OS   Wolbachia sp. subsp. Drosophila simulans (strain wRi).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia.
OX   NCBI_TaxID=66084 {ECO:0000313|EMBL:ACN95603.1, ECO:0000313|Proteomes:UP000001293};
RN   [1] {ECO:0000313|EMBL:ACN95603.1, ECO:0000313|Proteomes:UP000001293}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=wRi {ECO:0000313|Proteomes:UP000001293};
RX   PubMed=19307581; DOI=10.1073/pnas.0810753106;
RA   Klasson L., Westberg J., Sapountzis P., Naeslund K., Lutnaes Y.,
RA   Darby A.C., Veneti Z., Chen L., Braig H.R., Garrett R., Bourtzis K.,
RA   Andersson S.G.;
RT   "The mosaic genome structure of the Wolbachia wRi strain infecting
RT   Drosophila simulans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5725-5730(2009).
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:0000256|HAMAP-
CC       Rule:MF_00205}.
CC   -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for
CC       lesions. {ECO:0000256|HAMAP-Rule:MF_00205}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00205}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA family.
CC       {ECO:0000256|ARBA:ARBA00038000, ECO:0000256|HAMAP-Rule:MF_00205}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00205}.
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DR   EMBL; CP001391; ACN95603.1; -; Genomic_DNA.
DR   RefSeq; WP_012673297.1; NZ_MKIF01000055.1.
DR   AlphaFoldDB; C0R3W1; -.
DR   STRING; 66084.WRi_008740; -.
DR   KEGG; wri:WRi_008740; -.
DR   HOGENOM; CLU_001370_0_2_5; -.
DR   Proteomes; UP000001293; 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   CDD; cd03271; ABC_UvrA_II; 1.
DR   Gene3D; 3.30.190.20; -; 1.
DR   Gene3D; 1.10.8.280; ABC transporter ATPase domain-like; 2.
DR   Gene3D; 1.20.1580.10; ABC transporter ATPase like domain; 4.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR00630; uvra; 1.
DR   PANTHER; PTHR43152; UVRABC SYSTEM PROTEIN A; 1.
DR   PANTHER; PTHR43152:SF3; UVRABC SYSTEM PROTEIN A; 1.
DR   Pfam; PF17755; UvrA_DNA-bind; 1.
DR   Pfam; PF17760; UvrA_inter; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00205};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   DNA excision {ECO:0000256|ARBA:ARBA00022769, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   Excision nuclease {ECO:0000256|ARBA:ARBA00022881, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00205};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00205};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00205};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW   Rule:MF_00205}.
FT   DOMAIN          598..927
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   ZN_FING         730..756
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         32..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         631..638
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   931 AA;  103324 MW;  7D9F822200CEF687 CRC64;
     MDDFIRVKGA REHNLQGVDV NIPKNKLVVI TGLSGSGKSS LAFDTIYAEG QRRYVESLSA
     YARQFLNIQD KPDVESITGL SPAISINQKS ISKNPRSTVG TVTEIYDYLR LVYARIGVPY
     SPATGLPITK QTVSQIVDTI IALPLETKIY ILAPVVRGRK GEHLKEILEI KRQGYVRFKI
     DGEVYNVDDL PKLDKNKKHD VFVVADRISI LDDIGNRLPS SIESALKLGN GLMYVEIVNL
     PDNHNSEYKN GQILIFSENF ACPESGFTLE EIEPRLFSFN SPYGACGSCN GLGKKLAVDV
     KLIVPDETLS ISEGALKPVG SMFRQVHTSY GFLKSAILSL AENCKFSLDV PWKNIDQEVK
     DMILFGFGKF QGLVSILENQ MDYDETLVER YCSVTHCREC TGYRLRKEAL TVKIDSKHIG
     EISGLSIDES LKWFENLPDK LTEQQKQISS KILNEIIKRL AFLKNVGLNY LTLDRESSTL
     SGGESQRIRL ASQIGSGLTG VLYVLDEPSI GLHQCDNDRL IATLKNLRDM GNTVIVVEHD
     EDTIMAADYA IDIGPGAGVN GGKVVAEGTP DQVQRNSGSI TGQYLSGEKK ILIPRRRKQA
     TQFIKVINAC ENNLKNVNVK FPIGNLICVT GISGGGKSSL IIETLYKYSA HKIHHSSARY
     GQCDKIEGLE YVDKIIEVDQ SPIGRTPASN PATYVGMFTH IRNWFAGLPE SKARGYNIGR
     FSFNTRGGRC EACKGDGHLK IEMHFLPDVY VKCEQCKGRR YNRETLEVTY KEKSISDVLD
     MTIDQACVFF ENLPMVKEKL VSLQEVGLGY IKLGQSSTTL SGGEAQRIKL SKELSKRFTG
     RTLYILDEPT TGLHFEDINN LLKILHRLVD LGNTVIVIEH NLHVIKTADY IIDIGPEGGI
     KGGEVIATGT PEEVVKIPES VTGRYLKTYL L
//
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