ID A0A498DT25_9ACTN Unreviewed; 992 AA.
AC A0A498DT25;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
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:RLL66286.1};
GN ORFNames=D7M15_04610 {ECO:0000313|EMBL:RLL66286.1};
OS Streptomyces sp. Z26.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2500177 {ECO:0000313|EMBL:RLL66286.1, ECO:0000313|Proteomes:UP000288048};
RN [1] {ECO:0000313|EMBL:RLL66286.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z26 {ECO:0000313|EMBL:RLL66286.1};
RA Buchmann A., Cano-Prieto C., Baz M., Hassani L., Barakate M., Nafis A.,
RA Niedermeyer T.H.J., Gross H.;
RT "Draft Genome Sequence of the Novonestmycin-Producing Strain Streptomyces
RT sp. Z26, isolated from potato rhizosphere in Morocco.";
RL Submitted (OCT-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: 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:RLL66286.1}.
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DR EMBL; RCHV01000002; RLL66286.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498DT25; -.
DR OrthoDB; 9809851at2; -.
DR Proteomes; UP000288048; 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:UP000288048};
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 603..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 951..992
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 992 AA; 109053 MW; 724903EE45BA5431 CRC64;
MADRLSVRGA REHNLKNVSL DLPRDALIVF TGLSGSGKSS LAFDTIFAEG QRRYVESLSS
YARQFLGQMD KPDVDFIEGL SPAVSIDQKS TSRNPRSTVG TITEVYDYLR LLFARIGRPH
CPECGRPIAR QSPQAIVDKV LDLEPGTRFQ VLSPLVRERK GEFVDLFADL QTKGYSRARV
DGETVQLSEP PKLKKQEKHT IEVVVDRLTV KESAKRRLTD SVETALGLAG GMVILDFVDL
PADDPQRERM YSEHLYCPHD DLSFEEMEPR SFSFNSPFGA CPECTGIGTR MEVDPELIVP
DEDKSLDEGA IHPWSHGHTK DYFARLIGAL ADALGFRTDI PWAGLPQRAR KALLHGHRTQ
IEVRYRNRYG RERAYTTSFE GAVPFVRRRH QEAETDTSRE RFEGYMREVP CPSCAGTRLK
PVVLAVTVQD RSIADVAAMS ISECADFLGG MKLTDREKTI AERVLKEVNE RLRFLVDVGL
DYLSLNRAAG TLSGGEAQRI RLATQIGSGL VGVLYVLDEP SIGLHQRDNH RLMETLVRLR
DLGNTLIVVE HDEDTIKTSD WVVDIGPGAG EHGGEVVHSG TLKELLANEK SVTGQYLAGK
RQIPTPDVRR PLDPKRRLTV HGARENNLRD LTVSFPLGVL TAVTGVSGSG KSTLVNDILY
THLARELNGA KSVPGRHTRV DGDDLVDKVV HVDQSPIGRT PRSNPATYTG VFDHVRKLFA
ETMEAKVRGY QPGRFSFNVK GGRCENCSGD GTIKIEMNFL PDVYVPCEVC HGDRYNRETL
EVHYKGKSIA EVLDMPIEEA TDFFEAVPAI SRHLRTLKDV GLGYVRLGQP APTLSGGEAQ
RVKLASELQK RSTGRTVYVL DEPTTGLHFE DIRKLITVLS GLVDKGNTVI VIEHNLDVIK
TADWLVDMGP EGGSGGGLVV AEGTPEQVAG VTGSHTGKFL RDILGSRVTD APAELKPAGK
TAKKTTGAKA AKAAKTATGA KAAKKTAATR KR
//
