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Database: UniProt
Entry: A0A316F4N5_9BURK
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ID   A0A316F4N5_9BURK        Unreviewed;       954 AA.
AC   A0A316F4N5;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=C7419_1012491 {ECO:0000313|EMBL:PWK38593.1};
OS   Cupriavidus plantarum.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=942865 {ECO:0000313|EMBL:PWK38593.1, ECO:0000313|Proteomes:UP000245754};
RN   [1] {ECO:0000313|EMBL:PWK38593.1, ECO:0000313|Proteomes:UP000245754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SLV-132 {ECO:0000313|EMBL:PWK38593.1,
RC   ECO:0000313|Proteomes:UP000245754};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing
RT   to study the core and pangenomes of soil and plant-associated
RT   prokaryotes.";
RL   Submitted (MAY-2018) 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PWK38593.1}.
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DR   EMBL; QGGT01000001; PWK38593.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316F4N5; -.
DR   Proteomes; UP000245754; 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:UP000245754};
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          619..948
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         751..777
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         652..659
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   954 AA;  105341 MW;  F3DC04DA090E94FA CRC64;
     MEEIKIRGAR THNLKNINLD LPRNKLIVIT GLSGSGKSSL AFDTLYAEGQ RRYVESLSAY
     ARQFLQLMEK PDVDLIEGLS PAISIEQKAT SHNPRSTVGT VTEIHDYLRL LFARAGTPYC
     PDHNIALQAQ SVSQMVDAAL ALPEDTKLMI LAPVVADRKG EHSDLFDTMQ AQGFVRFRIR
     SGGGTAHEAE TKVFEVDQLP KLKKTEKHSI DVVVDRVKVR PDIKQRLAES FETALRLADG
     RAIALEMDTG HEHVFSSRFA CPICSYSLQE LEPRLFSFNN PMGACTTCDG LGQITFFDPK
     RVVAFPNLSL ASGAIKGWDR RNQFYFQMLQ SLAAFYDFDT ETAFEELPQK VQEVVLHGSG
     EEEIPFTYIN EKGRTTVRAH VFEGIIPNLE RRYRETDSIA VREELAKYQN NQPCPACHGT
     RLRTEARHVK VGEDDQARAI FEINAQPLRD ALTWFLTLNL HGAKREIADK IVKEITARLN
     FLNNVGLDYL SLERSADTLS GGEAQRIRLA SQIGSGLTGV MYVLDEPSIG LHQRDNDRLI
     GTLKHLRDIG NSVLVVEHDE DMIRASDYVV DIGPGAGVHG GMIVAEGTPG QIEASVASLT
     GQYLSGQRRI EVPAKRAAPD EERLLRIVNA TGNNLRNVTA EIPVGLLTCI TGVSGSGKST
     LINDTLYHAV ARHLYGSTPE PAAHDRIEGL EHFDKVINVD QSPIGRTPRS NPATYTGLFT
     PIRELFAGVP SAKERGYDPG RFSFNVKGGR CESCQGDGVI KVEMHFLPDV YVPCDVCHGQ
     RYNRETLEVL YKGKSISEVL DLTVEQAHEF FSAVPVVRRK LQTLLDVGLG YIRLGQSATT
     LSGGEAQRVK LSLELSKRDT GRTLYILDEP TTGLHFHDIE LLLKVIHKLR DQGNTVVIIE
     HNLDVIKTAD WLLDMGPEGG AGGGQVIAKG TPEAVAKSKA SFTGKYLAPL LKRG
//
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