UVRA_STRCO
ID UVRA_STRCO Reviewed; 1014 AA.
AC Q9Z507;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=UvrABC system protein A {ECO:0000255|HAMAP-Rule:MF_00205};
DE Short=UvrA protein {ECO:0000255|HAMAP-Rule:MF_00205};
DE AltName: Full=Excinuclease ABC subunit A {ECO:0000255|HAMAP-Rule:MF_00205};
GN Name=uvrA {ECO:0000255|HAMAP-Rule:MF_00205}; OrderedLocusNames=SCO1958;
GN ORFNames=SCC54.18c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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:0000255|HAMAP-
CC Rule:MF_00205}.
CC -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for
CC lesions. {ECO:0000255|HAMAP-Rule:MF_00205}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00205}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA family.
CC {ECO:0000255|HAMAP-Rule:MF_00205}.
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DR EMBL; AL939110; CAB38148.1; -; Genomic_DNA.
DR PIR; T36031; T36031.
DR RefSeq; NP_626222.1; NC_003888.3.
DR RefSeq; WP_011028066.1; NZ_VNID01000001.1.
DR AlphaFoldDB; Q9Z507; -.
DR SMR; Q9Z507; -.
DR STRING; 100226.SCO1958; -.
DR PRIDE; Q9Z507; -.
DR GeneID; 1097392; -.
DR KEGG; sco:SCO1958; -.
DR PATRIC; fig|100226.15.peg.1984; -.
DR eggNOG; COG0178; Bacteria.
DR HOGENOM; CLU_001370_0_2_11; -.
DR InParanoid; Q9Z507; -.
DR OMA; PFEGIIP; -.
DR PhylomeDB; Q9Z507; -.
DR Proteomes; UP000001973; 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 Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF17755; UvrA_DNA-bind; 1.
DR Pfam; PF17760; UvrA_inter; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00630; uvra; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA damage; DNA excision; DNA repair; DNA-binding;
KW Excision nuclease; Metal-binding; Nucleotide-binding; Reference proteome;
KW Repeat; SOS response; Zinc; Zinc-finger.
FT CHAIN 1..1014
FT /note="UvrABC system protein A"
FT /id="PRO_0000093098"
FT DOMAIN 314..592
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT DOMAIN 612..941
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT ZN_FING 744..770
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT REGION 976..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1014
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT BINDING 645..652
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
SQ SEQUENCE 1014 AA; 110998 MW; 084D6B18692A792D CRC64;
MADRLIVRGA REHNLKNVSL DLPRDSLIVF TGLSGSGKSS LAFDTIFAEG QRRYVESLSS
YARQFLGQMD KPDVDFIEGL SPAVSIDQKS TSRNPRSTVG TITEVYDYLR LLFARIGKPH
CPECGRPISR QSPQAIVDKV LELPEGSRFQ VLSPLVRERK GEFVDLFADL QTKGYSRARV
DGETVQLSNP PTLKKQEKHT IEVVVDRLTV KDSAKRRLTD SVETALGLSG GMVVLDFVDL
PEDDPERERM YSEHLYCPYD DLSFEELEPR SFSFNSPFGA CPDCSGIGTR MEVDAELIVP
DEDKSLDEGA IHPWSHGHTK DYFGRLIGAL ADALGFRTDI PFAGLPLRAR KALLYGHKTQ
VEVRYRNRYG RERRYTTAFE GAIPFVKRRH SEAESDASRE RFEGYMREVP CPTCQGTRLK
PLVLAVTVMG KSIAEVSAMS ISDCADFLGE LTLNARDKKI AERVLKEVNE RLRFLVDVGL
DYLSLNRAAG TLSGGEAQRI RLATQIGSGL VGVLYVLDEP SIGLHQRDNH RLIETLVRLR
DMGNTLIVVE HDEDTIKVAD WIVDIGPGAG EHGGKVVHSG SVKELLDNAE SQTGLYLSGR
KAIPLPDIRR PQDPSRRLTV HGARENNLQD IDVSFPLGVF TAVTGVSGSG KSTLVNDILY
THLARELNGA RNVPGRHTRV DGDDLVDKVV HVDQSPIGRT PRSNPATYTG VFDHIRKLFA
ETTEAKVRGY LPGRFSFNVK GGRCENCAGD GTIKIEMNFL PDVYVPCEVC HGARYNRETL
EVHYKGKSIA DVLNMPIEEA TDFFEAVPAI SRHMKTLKDV GLGYVRLGQS ATTLSGGEAQ
RVKLASELQR RSTGRTVYVL DEPTTGLHFE DISKLLTVLG GLVDKGNTVI VIEHNLDVIK
TADWVVDMGP EGGAGGGLVV AEGTPEQVAG VPASHTGKFL RDVLGADRVS DAAPVTRPRK
AAKTVAAKAA AKKTATKTVT GTAAKKATAT RTAKTAVKKA AKPAAKKTTR TSKA
