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Database: UniProt
Entry: A0A2U1AVX1_9BACT
LinkDB: A0A2U1AVX1_9BACT
Original site: A0A2U1AVX1_9BACT 
ID   A0A2U1AVX1_9BACT        Unreviewed;       952 AA.
AC   A0A2U1AVX1;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=C8D82_11627 {ECO:0000313|EMBL:PVY40576.1};
OS   Victivallis vadensis.
OC   Bacteria; Lentisphaerota; Lentisphaeria; Victivallales; Victivallaceae;
OC   Victivallis.
OX   NCBI_TaxID=172901 {ECO:0000313|EMBL:PVY40576.1, ECO:0000313|Proteomes:UP000245959};
RN   [1] {ECO:0000313|EMBL:PVY40576.1, ECO:0000313|Proteomes:UP000245959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14823 {ECO:0000313|EMBL:PVY40576.1,
RC   ECO:0000313|Proteomes:UP000245959};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (APR-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:PVY40576.1}.
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DR   EMBL; QEKH01000016; PVY40576.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U1AVX1; -.
DR   Proteomes; UP000245959; 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; 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; 4.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   HAMAP; MF_00205; UvrA; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
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   SMART; SM00382; AAA; 2.
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:UP000245959};
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          610..947
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   ZN_FING         260..287
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         32..39
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   952 AA;  105038 MW;  743DB4E1336B7DA7 CRC64;
     MFEKIQIRGA TQHNLKGIDV TIPRNKLVVI TGLSGSGKSS LAFDTLYAEG QRRYVESLSA
     YARQFLDRMQ KPKVEHIEGL SPAIAIEQRT AGGTPRSTVA TVTEIYDYLR LLYAHVGVPH
     CPHCGRKLQS QSAQAIAEQL LALKPGQKMM ILAPFVNGRK GEHRDVLDSI RSEGFVRARI
     DGDIVQFDEE ELPRLEKTRR HTIEAVVDRL ITGKLDRSRL TDSVETALRH GGGTIHVLLE
     APAGEKPDFE EEKFSENLAC PDCGVSYGEL LPRNFSFNSP YGACPECNGL GVQQVMDPLK
     VVPDPSLSIK NGAIPGWRRG PRHLIIYYNL LLRKLSEWLE EPDMLTTPFN KLPERVRNIV
     LYGTGDTPLE FDYRMHGKKY RWSKPFEGVL ENLRRRMTET ESDSVRERLG EYLSPRECPA
     CHGARLKPVS LAVTVGGLGI DKFNAQSVEA ALKFVSELEL DKEQAAIAGD VLKEIRSRLT
     FLCDVGLNYL TLDRVSSTLS GGEAQRIRLA TQLGCGLVGV LYILDEPSIG LHQRDNDRLL
     DTLEKLRDIG NTVLVVEHDL DTIERADYVL DLGPGAGVHG GELVAYGTPK ELVNFPRSLT
     ADFLAGRREI AVPDERRKGN GHKLVIRGAE FHNLRKLTAE IPLGTFTCVT GVSGSGKSSL
     INGILVRALN AHQGIQDLPP GKCKAVEGLE FVDKAIVIDQ SPIGRTPRSN PATYTDAFGG
     IRKLFSELPE SKVRGFGPGR FSFNVKGGRC EECKGDGIKK IEMQFLSDVY VECSACNGRR
     FNKETLGVHY KKKNIADVLD MTVNQAVEFF SAIPSLTRKF KTLQEVGLGY VTLGQPATTL
     SGGEAQRVKL AAELARVPRG HTVYILDEPT TGLHLADIDQ LLKVLFKLRD MGNTVIVIEH
     NLDVIKTADY LLDLGPEGGD RGGKLIASGT PEEVAKVKGS HTGRYLKKYL KK
//
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