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Database: UniProt
Entry: UVRA_STRAW
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ID   UVRA_STRAW              Reviewed;        1009 AA.
AC   Q829X3;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 126.
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=SAV_6286;
OS   Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS   14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=227882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC   8165 / MA-4680;
RX   PubMed=11572948; DOI=10.1073/pnas.211433198;
RA   Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA   Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M.;
RT   "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT   deducing the ability of producing secondary metabolites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC   8165 / MA-4680;
RX   PubMed=12692562; DOI=10.1038/nbt820;
RA   Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M., Omura S.;
RT   "Complete genome sequence and comparative analysis of the industrial
RT   microorganism Streptomyces avermitilis.";
RL   Nat. Biotechnol. 21:526-531(2003).
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; BA000030; BAC73997.1; -; Genomic_DNA.
DR   RefSeq; WP_010987687.1; NZ_JZJK01000089.1.
DR   AlphaFoldDB; Q829X3; -.
DR   SMR; Q829X3; -.
DR   KEGG; sma:SAVERM_6286; -.
DR   eggNOG; COG0178; Bacteria.
DR   HOGENOM; CLU_001370_0_2_11; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000000428; 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; PF00005; ABC_tran; 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; 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..1009
FT                   /note="UvrABC system protein A"
FT                   /id="PRO_0000093097"
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          956..1009
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        966..991
FT                   /note="Polar 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   1009 AA;  110787 MW;  CC90B4E219139700 CRC64;
     MADRLIVRGA REHNLKNVSL DLPRDSLIVF TGLSGSGKSS LAFDTIFAEG QRRYVESLSS
     YARQFLGQMD KPDVDFIEGL SPAVSIDQKS TSRNPRSTVG TITEVYDYLR LLFARIGKPH
     CPECGRPISR QSPQAIVDKV LELPEGSRFQ VLSPLVRERK GEFVDLFADL QTKGYSRARV
     DGQTIQLSDP PTLKKQEKHT IEVVIDRLTV KEGAKRRLTD SVETALGLAG GMVVLDFVDL
     PEDDPERERM YSEHLYCPYD DLSFEELEPR SFSFNSPFGA CPDCSGIGTR MEVDAELIVP
     DEEKSLDEGA IHPWSHGHTK DYFGRLIGAL ADALGFRTDI PFAGLPQRAK KALLYGHKTQ
     IEVRYRNRYG RERVYTTPFE GAVPFVKRRH SEAESDASRE RFEGYMREVP CPTCQGTRLK
     PLVLAVTVME KSIAEVAAMS ISDCADFLGK LKLNARDKKI AERVLKEVNE RLRFLVDVGL
     DYLSLNRAAG TLSGGEAQRI RLATQIGSGL VGVLYVLDEP SIGLHQRDNH RLIETLVRLR
     DMGNTLIVVE HDEDTIKVAD WIVDIGPGAG EHGGKVVHSG SLKELLANAE SQTGQYLSGK
     KSIPLPDIRR PRDPSRQLTV HGARENNLQD IDVSFPLGVL TAVTGVSGSG KSTLVNDILY
     THLARELNGA RSVPGRHTRV DGDDLVDKVV HVDQSPIGRT PRSNPATYTG VFDHVRKLFA
     ETTEAKVRGY LPGRFSFNVK GGRCENCSGD GTIKIEMNFL PDVYVPCEVC HGARYNRETL
     EVHYKGKSIA DVLNMPIEEA MHFFEAVPAI ARHLNTLNDV GLGYVRLGQS ATTLSGGEAQ
     RVKLASELQR RSTGRTVYVL DEPTTGLHFE DISKLLVVLS GLVDKGNTVI VIEHNLDVIK
     TADWVVDMGP EGGAGGGLVV AEGTPEEVAG VPTSHTGKFL REILDADRIS DAASVKAPRK
     TAARKTAAAK STTKKTATVR TTNNTATKKA AAVTKKTAPA KKTTRARKA
//
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