ID A0A0Q5V6N8_9ACTN Unreviewed; 981 AA.
AC A0A0Q5V6N8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=ASG36_17385 {ECO:0000313|EMBL:KQS56801.1};
OS Geodermatophilus sp. Leaf369.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1736354 {ECO:0000313|EMBL:KQS56801.1, ECO:0000313|Proteomes:UP000051830};
RN [1] {ECO:0000313|EMBL:KQS56801.1, ECO:0000313|Proteomes:UP000051830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf369 {ECO:0000313|EMBL:KQS56801.1,
RC ECO:0000313|Proteomes:UP000051830};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS56801.1, ECO:0000313|Proteomes:UP000051830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf369 {ECO:0000313|EMBL:KQS56801.1,
RC ECO:0000313|Proteomes:UP000051830};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:KQS56801.1}.
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DR EMBL; LMQA01000004; KQS56801.1; -; Genomic_DNA.
DR RefSeq; WP_055766836.1; NZ_LMQA01000004.1.
DR AlphaFoldDB; A0A0Q5V6N8; -.
DR STRING; 1736354.ASG36_17385; -.
DR Proteomes; UP000051830; 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:UP000051830};
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 613..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 REGION 955..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..39
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 981 AA; 107727 MW; F09482FCB35FB4DD CRC64;
MMDRLVVRGA REHNLKDVHL DLPRDAMIVF TGLSGSGKSS LAFDTIFAEG QRRYVESLSA
YARQFLGQMD KPDVDFIEGL SPAVSIDQKS TNRNPRSTVG TITEVYDYLR LLYARAGQPH
CPNCGKPIAR QTPQQIVDQV LEMTEGTRFQ VLAPVVRARK GEYVDLFSSL QTQGFSRVRV
DGVIHSLTEP PKLKKQEKHT IEVIVDRLTV KESAKRRLTD SVETALGLAG GLVVLDFVDL
EEGDPERERT FSEHLACIDD GLSFEALEPR SFSFNSPFGA CAECTGIGTR KEVDPELVVP
DPEKSLGEGA IAPWAGSMSN EYFTRLLTGL GDQIGFSMKT PWEQLPAKIQ KAVLHGSPDQ
VHVRYKNRYG RERSYYAAFE GVLPFLERRH EDTDSEFMRD KYEGYMRDVP CPVCHGTRLK
PEILAVKLDG RSIAEVTGLS IGDASEWLDA LTLGERERAI ADRVLKEIQA RLSFLVSVGL
DYLSLDRPAA TLAGGEAQRI RLATQIGSGL VGVLYVLDEP SIGLHQRDNV RLIETLVRLR
DMGNTLIVVE HDEDTIKQAD WIVDIGPGAG EHGGEVVVSG TYEDLLASER SLTGQYLSGR
KEIVIPAERR PRTPGRELVV KGAREHNLRG VDVTFPLGML VAVTGVSGSG KSSLVNDILY
TVLANQLNRA RMVPGRHRTI TGLDQLDKVV GVDQSPIGRT PRSNPATYTG VWDAIRKLFA
STEEAKVRGY QPGRFSFNVK GGRCEACSGD GTLKIEMNFL PDVYVPCEVC KGARFNRETL
EVRYKNKTVA EVLDMPIEEA AEFFAPINSI ARYLTTLTEV GLGYVRLGQP ATTLSGGEAQ
RVKLASELQK RSNGRTIYVL DEPTTGLHFE DIRKLLLVIQ GLVDKGNSVI VIEHNLDVIK
SADWLIDMGP EGGFRGGTVV GEGTPELIAG IPESHTGKFL AEILDPARME AAAKKKPRKK
VAASAPAADV VTDPVSAGRT V
//
