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Database: UniProt
Entry: A0A344U9W8_9ACTN
LinkDB: A0A344U9W8_9ACTN
Original site: A0A344U9W8_9ACTN 
ID   A0A344U9W8_9ACTN        Unreviewed;       991 AA.
AC   A0A344U9W8;
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   ORFNames=C0216_22840 {ECO:0000313|EMBL:AXE27689.1};
OS   Streptomyces globosus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=68209 {ECO:0000313|EMBL:AXE27689.1, ECO:0000313|Proteomes:UP000252004};
RN   [1] {ECO:0000313|EMBL:AXE27689.1, ECO:0000313|Proteomes:UP000252004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LZH-48 {ECO:0000313|EMBL:AXE27689.1,
RC   ECO:0000313|Proteomes:UP000252004};
RA   Ran K., Li Z., Wei S., Dong R.;
RT   "Draft genome Sequence of streptomyces globosus LZH-48.";
RL   Submitted (JAN-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}.
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DR   EMBL; CP030862; AXE27689.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A344U9W8; -.
DR   KEGG; sgz:C0216_22840; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000252004; Chromosome.
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:UP000252004};
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          949..991
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   991 AA;  108883 MW;  7D7F2B3C5A4C4682 CRC64;
     MTDRLIVRGA REHNLKNVSL DLPRDSLIVF TGLSGSGKSS LAFDTIFAEG QRRYVESLSS
     YARQFLGQMD KPDVDFIEGL SPAVSIDQKS TSRNPRSTVG TITEVYDYLR LLFARIGKPH
     CPECRRPISR QSPQAIVDKV LALPEGSRFQ VLSPLVRERK GEFVDLFADL QTKGYSRARV
     DGTTVQLSEP PVLKKQEKHT IEVVVDRLTV KESAKRRLTD SVETALGLSG GMVILDFVDL
     AEDDPERERM FSEHLYCPYD DLSFEELEPR SFSFNSPFGA CPECTGIGTR MEVDPELIVP
     DEEKSLDEGA VSPWSLGHTK DYFQRLVGAL ADELGFRTDI PWAGLPQRAK KALLYGHKTQ
     IEVRYRNRYG RERAYTTAFE GAVPFVRRRH AESESDASRE RFEGYMREVP CPTCRGTRLK
     PIVLAVTVME RSIAEVAAMS ISECADFLGR LRLDARDKKI AERVLKEVNE RLRFLVDVGL
     DYLSLNRAAG TLSGGEAQRI RLATQIGSGL VGVLYVLDEP SIGLHQRDNH RLIETLVRLR
     DMGNTLIVVE HDEDTIKVAD WVVDIGPGAG EHGGKVVHSG SLAELLENGS SMTGQYLSGK
     KSIPVPEIRR PVNGDRRLTV HGAKENNLRD IDVSFPLGVL TAVTGVSGSG KSTLVNDILY
     THLARELNGA RSVPGRHTRV EGDDLVDKVV HVDQSPIGRT PRSNPATYTG VFDNIRKLFA
     ETMEAKVRGY LPGRFSFNVK GGRCENCSGD GTIKIEMNFL PDVYVPCEVC HGDRYNRETL
     EVHYKGKSIA EVLNMPIEEA LGFFEAVPTI SRHLKTLTEV GLGYVRLGQS APTLSGGEAQ
     RVKLASELQK RSTGRTVYVL DEPTTGLHFE DISKLIKVLS GLVDKGNSVI VIEHNLDVIK
     TADWVIDMGP EGGHGGGMVV AEGTPEQVAS VGASHTGKFL RDILGADRVS DAGPSAAPVR
     KAAAKKTAAR KTAAPARKAA AKKAAPKARK A
//
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