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Database: UniProt
Entry: A0A1Y5R8Q3_9RHOB
LinkDB: A0A1Y5R8Q3_9RHOB
Original site: A0A1Y5R8Q3_9RHOB 
ID   A0A1Y5R8Q3_9RHOB        Unreviewed;       955 AA.
AC   A0A1Y5R8Q3;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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:SLN11349.1};
GN   ORFNames=PSA7680_00128 {ECO:0000313|EMBL:SLN11349.1};
OS   Pseudoruegeria aquimaris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Pseudoruegeria.
OX   NCBI_TaxID=393663 {ECO:0000313|EMBL:SLN11349.1, ECO:0000313|Proteomes:UP000193409};
RN   [1] {ECO:0000313|EMBL:SLN11349.1, ECO:0000313|Proteomes:UP000193409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7680 {ECO:0000313|EMBL:SLN11349.1,
RC   ECO:0000313|Proteomes:UP000193409};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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; FWFQ01000001; SLN11349.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y5R8Q3; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000193409; Unassembled WGS sequence.
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; cd03270; ABC_UvrA_I; 1.
DR   CDD; cd03271; ABC_UvrA_II; 1.
DR   Gene3D; 1.10.8.280; ABC transporter ATPase domain-like; 1.
DR   Gene3D; 1.20.1580.10; ABC transporter ATPase like domain; 2.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   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}; Reference proteome {ECO:0000313|Proteomes:UP000193409};
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          601..941
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   ZN_FING         744..770
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         34..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         645..652
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   955 AA;  106074 MW;  D06E074BDCA238EC CRC64;
     MPELKKIEVR GAREHNLKSI DVDIPRDELV VITGLSGSGK SSLAFDTIYA EGQRRYVESL
     SAYARQFLDM MEKPDVDHIA GLSPAISIEQ KTTSKNPRST VGTVTEIYDY LRLLFARVGT
     PYSPATGLPI EAQQVQDMVD RVMGMEEGTR AYLLAPIVRD RKGEYRKEFM ELRKQGFQRV
     KVDGDFYELD EPPTLDKKFR HDIDVVVDRI VVREGMETRL ADSFRTALDL ADGIAILETA
     PKEGEPERIT FSEKFACPVS GFTIPEIEPR LFSFNAPFGA CPSCDGLGME LFFDERLVVP
     DATLKLYDGA LAPWRKGKSP YFLQTIEAIA RHYEFDKNTP WKDLPAHVQQ VFLYGSGEDE
     IRFRYDEGGR VYEVTRSFEG VIPNMERRYR ETDSNWIREE FERYQNNRPC GDCGGYRLRE
     EALAVKIAGL HIGQVVQMSI REAFDWCQTV PESLTAQKNE IARAILKEIR ERLGFLNNVG
     LEYLTLSRSA GTLSGGESQR IRLASQIGSG LTGVLYVLDE PSIGLHQRDN DRLLGTLKNL
     RDQGNTVIVV EHDEEAIREA DYVFDIGPGA GVHGGQVVAQ GTPAQIAADP ASLTGQYLSG
     ARAIDVPAER RKGNKKKITV VKASGNNLKD VTVDFPLGKF VCVTGVSGGG KSTLTIETLF
     KTASMRLNGA RQTPAPCETI KGLEHLDKVI DIDQRPIGRT PRSNPATYTG AFTPIRDWFA
     GLPEAKTRGY KPGRFSFNVK GGRCEACQGD GVIKIEMHFL PDVYVTCETC GGARYNRETL
     EIKFKGKSIA DVLDMTVEDA KEFFQAVPSI REKMEALSRV GLDYIKVGQQ ATTLSGGEAQ
     RVKLSKELAK RSTGRTLYIL DEPTTGLHFE DVRKLLEVLH ELVDQGNTVV VIEHNLDVVK
     TADWVIDIGP EGGDGGGEVV AVGTPEDIVK EPRSHTGRYL KELLEAGARR RVAAE
//
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