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Database: UniProt
Entry: A0A377KQ46_9ENTE
LinkDB: A0A377KQ46_9ENTE
Original site: A0A377KQ46_9ENTE 
ID   A0A377KQ46_9ENTE        Unreviewed;       938 AA.
AC   A0A377KQ46;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
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:STP30484.1};
GN   ORFNames=NCTC8129_02730 {ECO:0000313|EMBL:STP30484.1};
OS   Enterococcus durans.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=53345 {ECO:0000313|EMBL:STP30484.1, ECO:0000313|Proteomes:UP000254070};
RN   [1] {ECO:0000313|EMBL:STP30484.1, ECO:0000313|Proteomes:UP000254070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC8129 {ECO:0000313|EMBL:STP30484.1,
RC   ECO:0000313|Proteomes:UP000254070};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-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}.
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DR   EMBL; UGIF01000002; STP30484.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A377KQ46; -.
DR   Proteomes; UP000254070; 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:0022857; F:transmembrane transporter activity; IEA:UniProt.
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; 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; PF00005; ABC_tran; 1.
DR   Pfam; PF17755; UvrA_DNA-bind; 1.
DR   Pfam; PF17760; UvrA_inter; 1.
DR   SMART; SM00382; AAA; 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          602..934
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   ZN_FING         252..279
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   ZN_FING         737..763
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         33..40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         638..645
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   938 AA;  103904 MW;  A3417CA3D4E82C28 CRC64;
     MANDKIIIHG ARAHNLKNVN VTIPRDKFVV VTGLSGSGKS SLAFDTLYAE GQRRYVESLS
     AYARQFLGQM DKPDVDSIDG LSPAISIDQK TTSKNPRSTV GTVTEINDYL RLLFARVGHP
     ICPNDHIEIT SQSVDQMADQ VLELPERTKI QVLAPIIVKK KGQHKKVFER IQKEGYVRVR
     VDGEIYDLSE VPELEKNKKH DIAIVIDRIV IKEGIRSRLF DSIEAALRLA DGYVLVDVIG
     EDEMLFSEHY SCPYCGFTVG ELEPRLFSFN APFGACPDCD GLGVKLEVDQ DLVIPDRTKT
     LSQGAIIPWN PISSQYYPQM LAQACESNGI DMDTTFEELP TEHQEIILNG TDEIFHFHYE
     NDFGGVRDVE TTFEGVLKNI KRRYHDTNSD FTREQMRQYM TELTCQTCKG YRLNPQALSV
     QINGTNIGQT NELSIQKAVN FFSTLTLSEQ EKIIARPILK EVNDRLSFLE NVGLDYLTLS
     RASGTLSGGE AQRIRLATQI GSNLSGVLYI LDEPSIGLHQ RDNDRLIGSL KKMRDLGNTL
     VVVEHDEDTM RAADYLIDVG PGAGHQGGEI VAAGTPAEVA ADEHSLTGQY LSGKKRISVP
     KTRRKGNGKA IKITGATENN LKNVSVEFPL GEFVAVTGVS GSGKSTLVNS ILKRALAQKI
     NRNSAKPGKF KTITGYDSIE KIIDIDQSPI GRTPRSNPAT YTSVFDDIRD LFAKTNEAKM
     RGYKKGRFSF NVKGGRCEAC RGDGIIKIEM HFLPDVYVPC EVCHGKRYNS ETLEVHYKGK
     SIADILEMTV EDAVEFFEPI PKIRRKLQTI VDVGLGYVTM GQPATKLSGG EAQRMKLASE
     LHKISNGKNF YILDEPTTGL HTDDIARLLD VLQRLVDAGN TVLVIEHNLD VIKTADHIID
     LGPEGGEGGG TILATGTPEE LIKVKESYTG RYLKKVMD
//
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