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Database: UniProt
Entry: A0A1C4SWU0_9ACTN
LinkDB: A0A1C4SWU0_9ACTN
Original site: A0A1C4SWU0_9ACTN 
ID   A0A1C4SWU0_9ACTN        Unreviewed;      1014 AA.
AC   A0A1C4SWU0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=GA0115242_145318 {ECO:0000313|EMBL:SCE51457.1};
OS   Streptomyces sp. SolWspMP-5a-2.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1838281 {ECO:0000313|EMBL:SCE51457.1, ECO:0000313|Proteomes:UP000199131};
RN   [1] {ECO:0000313|EMBL:SCE51457.1, ECO:0000313|Proteomes:UP000199131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SolWspMP-5a-2 {ECO:0000313|EMBL:SCE51457.1,
RC   ECO:0000313|Proteomes:UP000199131};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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; FMCI01000385; SCE51457.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C4SWU0; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000199131; 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};
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..1014
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   1014 AA;  110787 MW;  323B4CC9FCC9916D CRC64;
     MADRLIVRGA REHNLKNVSL DLPRDSLIVF TGLSGSGKSS LAFDTIFAEG QRRYVESLSS
     YARQFLGQMD KPDVDFIEGL SPAVSIDQKS TSRNPRSTVG TITEVYDYLR LLFARIGKPH
     CPECGRPISR QSPQAIVDRV LELPEGSRFQ VLSPLVRERK GEFVDLFADL QTKGYSRARV
     DGATIQLAEP PTLKKQEKHT IEVVVDRLTV KDTAKRRLTD SVETALGLSG GMVVLDFVDL
     PEDDPERERM YSEHLYCPYD DLSFEELEPR SFSFNSPFGA CPDCSGIGTR MEVDPELIVP
     DEDKSLDEGA IHPWSHGHTK DYFGRLVGAL ADALGFRTDI PFAGLPLRAR KALLQGHKTQ
     IEVRYRNRYG RERVYTTPFE GAVPFVKRRH SEADSDASRE RFEGYMREVP CPTCEGTRLK
     PIVLAVTVMG KSIAEVSGMS ISDCADFLGE LRLNARDKRI AERVLKEVNE RLRFLVDVGL
     DYLSLNRAAG SLSGGEAQRI RLATQIGSGL VGVLYVLDEP SIGLHQRDNH RLIETLVRLR
     DMGNTLIVVE HDEDTIKIAD WIVDIGPGAG EHGGKVVHSG SYKELLDNAE SQTGLYLAGK
     KAIPLPDVRR PQDPSRRLTV HGARENNLQD IDVSFPLGVF TAVTGVSGSG KSTLVNDILY
     THLARELNGA RSVPGRHTRV AGDDLVDKVV HVDQSPIGRT PRSNPATYTG VFDHIRKLFA
     ETTEAKVRGY LPGRFSFNVK GGRCENCAGD GTIKIEMNFL PDVYVPCEVC HGARYNRETL
     EVHYKGKSIA EVLNMPIEEA RDFFEAVPAI SRHLGTLNDV GLGYVRLGQS ATTLSGGEAQ
     RVKLASELQR RSTGSTVYVL DEPTTGLHFE DISKLLTVLS GLVDKGNTVI VIEHNLDVIK
     TADWVVDMGP EGGAGGGLVV AEGTPEEVAG VPASHTGKFL RDILDADRIS DAPPSKAPRR
     TTTAKKAAVK KTATAAAGKT AVAAKKEPAA TKASGGAAKK TAAKKAASAR TRKS
//
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