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Database: UniProt
Entry: A0A162U0E5_9CLOT
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ID   A0A162U0E5_9CLOT        Unreviewed;       940 AA.
AC   A0A162U0E5;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
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_1 {ECO:0000313|EMBL:KZL93280.1};
GN   Synonyms=uvrA {ECO:0000256|HAMAP-Rule:MF_00205};
GN   ORFNames=CLMAG_03030 {ECO:0000313|EMBL:KZL93280.1};
OS   Clostridium magnum DSM 2767.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121326 {ECO:0000313|EMBL:KZL93280.1, ECO:0000313|Proteomes:UP000076603};
RN   [1] {ECO:0000313|EMBL:KZL93280.1, ECO:0000313|Proteomes:UP000076603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2767 {ECO:0000313|EMBL:KZL93280.1,
RC   ECO:0000313|Proteomes:UP000076603};
RA   Poehlein A., Uhlig R., Fischer R., Bahl H., Daniel R.;
RT   "Genome sequence of Clostridium magnum DSM 2767.";
RL   Submitted (APR-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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZL93280.1}.
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DR   EMBL; LWAE01000001; KZL93280.1; -; Genomic_DNA.
DR   RefSeq; WP_066616924.1; NZ_LWAE01000001.1.
DR   AlphaFoldDB; A0A162U0E5; -.
DR   STRING; 1121326.CLMAG_03030; -.
DR   PATRIC; fig|1121326.3.peg.280; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000076603; 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; 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; 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:UP000076603};
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          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;  104415 MW;  AE14BE0F47DF4F6A CRC64;
     MKDSIIIKGA KVHNLKNVDL EIPRDKLVIF TGLSGSGKSS LAFDTLYAEG QRRYVESLSA
     YARQFLGQMN KPDVEYIEGL SPAISIDQKT TSRNPRSTVG TVTEIYDYIR LLYARIGTPH
     CPKCGKEITQ QTVDQMIDKI LSMEERTKIQ ILSPIIRGRK GEHVKVLENI KKNGFVRARI
     DGETVDLEEE EVKLEKNIKH SIEVVIDRLI VKDDIRSRLA DSLETALKLS EGLVIVNVIG
     GEDILFSENF ACVDCGISIG EITPRMFSFN SPFGKCDRCD GLGTLMEIDP DLVIPDKSKS
     ILDGAVVTFG EGSLKEDSWT FSILKALSKK YKFKLDTPIE KLSPEIIDIL LYGLGGDKVK
     VNYTKDNRVV EFNHAFEGII NNLKRRYLES NSDYIKGEIE NYMSDNPCPK CKGARLKAEA
     LAVIVGGKNI DEFSKMSIRD ELKFLNDLQL SEKNKIISEQ ILKEIKSRLK FLIDVGLDYL
     NLTRTAGTLS GGEAQRIRLA TQIGSSLVGV LYILDEPSIG LHQRDNDKLI ATLKHLRDLG
     NTLVVVEHDE DTMKEADFIV DIGPGAGEHG GEIVAAGPIE EIIKNEKSIT GQYLSGTKKI
     ETPSTRREGN GNCLVVKGAK ENNLKNVNVS FPLGTLTCVT GVSGSGKSTL VNEILFKGLN
     KRINKSKDNP GFHKDITGVE NIDKIINIDQ SPIGRTPRSN PATYTGVFDI IREVFSNTSE
     AKMRGYKPGR FSFNVKGGRC EACSGDGIIK IEMQFLSDVY VPCEVCKGKR YNRETLEVKY
     KAKNIDDVLN MTVEEALVFF ENIPRIKNKL QTLFDVGLGY VRLGQPSTQL SGGEAQRIKL
     AYELSKRSTG KTLYILDEPT TGLHIDDVNR LIDILQRIVD TGNTVIVIEH NLDVIKCADY
     IIDLGPEGGE KGGTILFSGR PEEIVRNKSS YTGQYLKKML
//
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