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Database: UniProt
Entry: A0A1M6TW30_9CLOT
LinkDB: A0A1M6TW30_9CLOT
Original site: A0A1M6TW30_9CLOT 
ID   A0A1M6TW30_9CLOT        Unreviewed;       940 AA.
AC   A0A1M6TW30;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=SAMN02745163_04127 {ECO:0000313|EMBL:SHK61018.1};
OS   Clostridium cavendishii DSM 21758.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121302 {ECO:0000313|EMBL:SHK61018.1, ECO:0000313|Proteomes:UP000184310};
RN   [1] {ECO:0000313|EMBL:SHK61018.1, ECO:0000313|Proteomes:UP000184310}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21758 {ECO:0000313|EMBL:SHK61018.1,
RC   ECO:0000313|Proteomes:UP000184310};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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}.
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DR   EMBL; FQZB01000021; SHK61018.1; -; Genomic_DNA.
DR   RefSeq; WP_072992776.1; NZ_FQZB01000021.1.
DR   AlphaFoldDB; A0A1M6TW30; -.
DR   STRING; 1121302.SAMN02745163_04127; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000184310; 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; 1.
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:UP000184310};
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          600..937
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   ZN_FING         252..279
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   ZN_FING         740..766
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         641..648
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   940 AA;  104898 MW;  A5DBFACB5217CF3F CRC64;
     MKDKIVIKNA KVHNLKNVSL EIPRDKLVVF TGLSGSGKSS LAFDTLYAEG QRRYVESLSA
     YARQFLGQMN KPDVEAIEGL SPAISIDQKT TSKNPRSTVG TVTEIYDYLR LLYARVGIPH
     CPKCGKEITQ QTVDQIVDQV MSLPERTKIQ VLAPIVRGRK GTHEKMLENI KKSGYVRARI
     DGEIYDLTED EIKLEKNNKH NIEAVIDRLI VKPEIEGRLT DSIEASLKLA DGLVVINIIG
     EEDRLYSENF ACADCGISID ELAPRLFSFN SPFGKCNHCD GLGTLLEIDE DLIIPNKELS
     IMDGAIASWG EGRLKEDSWT YAILKALSKK YKFDLKTPIK DLPKEIYNIL LYGTKGEKVI
     VEYTKEGIKG KYNHSFEGEI NGLRRRYMET NSDYIKSEIE QYMSNNPCPK CKGARLKPEA
     LAVTVGDKNI NQFTRLSIRD ELEFINSIEF SEKNKIISNQ IVKEINSRLK FLIDVGLDYL
     DLARNSGTLS GGEAQRIRLA TQIGSQLMGV LYILDEPSIG LHQRDNDRLI ATLKHLRDIG
     NTLIVVEHDE DTMRAADFIV DIGPRAGEHG GEIIAAGPLE VIEATEESLT GQYLTGKKKV
     ELPEDRRKGN GNFLTIKGAK ENNLKNVNVK LPLGTLTMVT GVSGSGKSTL INEILFKGLT
     KIINKSKVNP GQYKEIIGYE NIDKIIDIDQ SPIGRTPRSN PATYTGTFDI IRELFSNTTE
     AKMRGYKQGR FSFNVKGGRC EACSGDGIIK IEMQFLSDVY VPCEVCKGKR YNRETLEVKY
     KGKNIDDVLN MTVGEALEFF ENIPRIKNKL QTLYDVGLGY IRLGQPSTQL SGGEAQRIKL
     AYELSKRNTG KTLYILDEPT TGLHVDDVNR LVQILQRLVD GGNSVVVIEH NLDMIKCADY
     IVDLGPEGGD KGGTIIATGT PEDICKVEES YTGKYLKKYL
//
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