ID A0A0G3ET32_9BURK Unreviewed; 954 AA.
AC A0A0G3ET32;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
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 ORFNames=ABW99_14170 {ECO:0000313|EMBL:AKJ69184.1};
OS Pandoraea thiooxydans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Pandoraea.
OX NCBI_TaxID=445709 {ECO:0000313|EMBL:AKJ69184.1, ECO:0000313|Proteomes:UP000036700};
RN [1] {ECO:0000313|Proteomes:UP000036700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25325 {ECO:0000313|Proteomes:UP000036700};
RA Lim Y.L., Ee R., Yong D., How K.Y., Yin W.F., Chan K.G.;
RL Submitted (JUN-2015) 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}.
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DR EMBL; CP011568; AKJ69184.1; -; Genomic_DNA.
DR RefSeq; WP_047215081.1; NZ_CP014839.1.
DR AlphaFoldDB; A0A0G3ET32; -.
DR STRING; 445709.ABW99_14170; -.
DR KEGG; ptx:ABW99_14170; -.
DR PATRIC; fig|445709.3.peg.3005; -.
DR OrthoDB; 9809851at2; -.
DR Proteomes; UP000036700; 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; cd03270; ABC_UvrA_I; 1.
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; 1.
DR Gene3D; 1.20.1580.10; ABC transporter ATPase like domain; 3.
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}; Reference proteome {ECO:0000313|Proteomes:UP000036700};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00205};
KW SOS response {ECO:0000256|HAMAP-Rule:MF_00205};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
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 618..947
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT ZN_FING 261..288
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT ZN_FING 750..776
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT BINDING 651..658
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ SEQUENCE 954 AA; 105475 MW; 38943425C138547D CRC64;
METIRIRGAR THNLKNINLD LPRHQLIVIT GLSGSGKSSL AFDTLYAEGQ RRYVESLSAY
ARQFLQLMEK PDVDLIEGLS PAISIEQKAT SHNPRSTVGT VTEIHDYLRL LYARVGTPHC
PDHGQPLESQ SVSQMVDAAL ALPADTKLMI LAPVVANRKG EHADLFDTMQ AQGFVRFRIR
SGGGAAHEGE AKIHEIDNLP RLKKNDKHSI DVVIDRVKVR DDLKQRLAES FETALRLADG
RAIAVEMDNG KEHVFSSKFA CPICSYSLQE LEPRLFSFNN PMGACPSCDG LGQMTFFDPK
RVVAFPGLSL ASGAVKGWDR RNQFYFQMLQ NLAAFYDFDV DTPFEELSET VQKTVLYGSD
KQTIPFTYVN ERGRTTVREH AFEGIIPSLE RRYRETDSLA VREELAKYQN NRPCPDCDGT
RLRREARFVK IGDGPKARAI YEINVWPLRE TLGYFHTLTL TGAKRDIADK IIKEIVARLT
FLNNVGLDYL SLERSADTLS GGEAQRIRLA SQIGSGLTGV MYVLDEPSIG LHQRDNDRLI
ATLKHLRDLG NSVIVVEHDE DMIRASDYVV DMGLGAGEHG GKVIAEGTPG QIAAHDVSLT
GQYLAGKRKI ALPAQRHAPG EHRLRISEAS GNNLKQVTLD LPVGLLTCVT GVSGSGKSTL
VNDTLYHAVA RHLYGSSAEP APFEAIDGLE HFDKVIAVDQ SPIGRTPRSN PATYTGLFTP
IRELFAGVPA AKERGYDPGR FSFNVKGGRC EACQGDGVLK VEMHFLPDVY VSCDVCHGKR
YNRETLEIQY KGKNIHEVLD MTVEQAHEFF RPVPVVARKL KTLLDVGLGY IRLGQSATTL
SGGEAQRVKL SLELSKRDTG RTLYILDEPT TGLHFHDIEL LLTVIHRLRD QGNTVVIIEH
NLDVIKTADW VIDLGPEGGA GGGRIIAYGT PEEVAGNKAS FTGKYLAPLL ERDR
//
