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Entry: D1A1R9_THECD
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ID   D1A1R9_THECD            Unreviewed;       946 AA.
AC   D1A1R9;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   24-JAN-2024, entry version 90.
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   OrderedLocusNames=Tcur_2191 {ECO:0000313|EMBL:ACY97757.1};
OS   Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC
OS   9072 / NBRC 15933 / NCIMB 10081 / Henssen B9).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Thermomonospora.
OX   NCBI_TaxID=471852 {ECO:0000313|EMBL:ACY97757.1, ECO:0000313|Proteomes:UP000001918};
RN   [1] {ECO:0000313|EMBL:ACY97757.1, ECO:0000313|Proteomes:UP000001918}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 /
RC   NCIMB 10081 / Henssen B9 {ECO:0000313|Proteomes:UP000001918};
RX   PubMed=21475583; DOI=10.4056/sigs.1453580;
RA   Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., Del Rio T.G.,
RA   Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Brettin T., Han C., Detter J.C., Rohde M., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Thermomonospora curvata type strain (B9).";
RL   Stand. Genomic Sci. 1:13-22(2011).
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; CP001738; ACY97757.1; -; Genomic_DNA.
DR   RefSeq; WP_012852541.1; NC_013510.1.
DR   AlphaFoldDB; D1A1R9; -.
DR   STRING; 471852.Tcur_2191; -.
DR   KEGG; tcu:Tcur_2191; -.
DR   eggNOG; COG0178; Bacteria.
DR   HOGENOM; CLU_001370_0_2_11; -.
DR   OMA; PFEGIIP; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000001918; 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; IPR003593; AAA+_ATPase.
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   SMART; SM00382; AAA; 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:UP000001918};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00205};
KW   SOS response {ECO:0000256|ARBA:ARBA00023236, ECO:0000256|HAMAP-
KW   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          613..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   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   946 AA;  104587 MW;  EC57FFEFEAB2E111 CRC64;
     MHDRLIVRGA REHNLKDVSL ELPRDSLIVF TGLSGSGKSS LAFDTIFAEG QRRYVESLSA
     YARQFLGQMD KPDVDFIEGL SPAVSIDQKS TSKNPRSTVG TITEVYDYLR LLYARIGRPH
     CPECGRPISR QTPQQIVDRV LELEPGTRFQ VLAPVIRGRK GEYAELFREL QSKGYSRALV
     DGVMVRLDDP PKLKKQEKHD IAVVVDRLTV KDSARRRLAD SVETALGLAG GTIVLDFVDL
     PEDDERRTRM FSEHLYCPYD DLSFEELEPR SFSFNSPYGA CPECTGLGTR MEVDPELVVP
     DPEKTLAEGA IQPWSNGHVS EYFLRLLSAL GDAMGFTLDT PWEKLPAKVR RAILKGYDTQ
     VHVSYKNRYG RTRSYYTTYE GVIPYIHRRH AESESDATRE RFEGYMRQVP CPACDGARLK
     PSVLAVTVGG KSIAEVAAMP ISECAEFLRT LELDDREAHI AARVLKEVNA RLGFLLDVGL
     DYLTLDRPAA TLAGGEAQRI RLATQIGSGL VGVLYVLDEP SIGLHQRDNH RLLETLLRLR
     DMGNTLIVVE HDEDTIAAAD WVVDIGPGAG EHGGQIVVSG PVEELKASPK SITGAYLSGR
     RRIEVPQVRR PRTKGREIVV RGAQQNNLKN IDVTFPLGVF TAVTGVSGSG KSTLVNDILY
     NALAKELHGA RTVPGKHRRI TGLEHVDKVV HVDQSPIGRT PRSNPATYTG VFDHIRKLFA
     ATPEAKVRGY QPGRFSFNVK GGRCENCAGD GTIKIEMNFL PDVYVPCEVC HGARYNRETL
     EVRYKGKTIA EVLDMPIEEA TRFFEPISAI HRHLSTLNDV GLGYVRLGQP APTLSGGEAQ
     RVKLAAELQR RSTGRTIYVL DEPTTGLHFE DIRKLLGVLN GLVDKGNTVV VIEHNLDVIK
     TADWIIDMGP EGGSRGGTVV AAGTPEEVAR VEASHTGRFL AKLLDR
//
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