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Database: UniProt
Entry: A0A151ALG4_9CLOT
LinkDB: A0A151ALG4_9CLOT
Original site: A0A151ALG4_9CLOT 
ID   A0A151ALG4_9CLOT        Unreviewed;       940 AA.
AC   A0A151ALG4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
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   ECO:0000313|EMBL:KYH28479.1};
GN   ORFNames=CLCOL_19710 {ECO:0000313|EMBL:KYH28479.1};
OS   Clostridium colicanis DSM 13634.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121305 {ECO:0000313|EMBL:KYH28479.1, ECO:0000313|Proteomes:UP000075374};
RN   [1] {ECO:0000313|EMBL:KYH28479.1, ECO:0000313|Proteomes:UP000075374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13634 {ECO:0000313|EMBL:KYH28479.1,
RC   ECO:0000313|Proteomes:UP000075374};
RA   Poehlein A., Daniel R.;
RT   "Genome sequence of Clostridium colicanis DSM 13634.";
RL   Submitted (FEB-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:KYH28479.1}.
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DR   EMBL; LTBB01000010; KYH28479.1; -; Genomic_DNA.
DR   RefSeq; WP_061858793.1; NZ_LTBB01000010.1.
DR   AlphaFoldDB; A0A151ALG4; -.
DR   STRING; 1121305.CLCOL_19710; -.
DR   PATRIC; fig|1121305.3.peg.1974; -.
DR   Proteomes; UP000075374; 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:UP000075374};
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          606..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;  104988 MW;  D367F1E3E45AFE3C CRC64;
     MRDKIVIKGA KVNNLQNVDL EIPRDKLVVF TGLSGSGKSS LAFDTLYAEG QRRYIESLSA
     YARQFLGQMD KPDVEYIEGL SPAISIDQKT TSRNPRSTVG TVTEIYDYLR LLYARVGIPH
     CPKCGREITQ QSVDTMIDKI LELPERSKVQ ILSPIINGRK GQHVKVLEDI KKNGFVRARI
     DGEIYDLQEE EVNLDKNKKH TIEAVIDRLI IKEGIESRLT DSLETALKLS EGVVIVNVIG
     GEDLKFSEKF ACPDCGISIS EIEPRLFSFN TPFGRCEKCD GIGSLMEIDE DLIIPDKSKS
     ILEGAIISLG DASLKEDSWT FSVLKALARE LKFDLNTPIE ELPRKTLDCI LYGLDGDKIT
     VEYVKEDKRG LYDHRYEGII NNLRRRYMET NSDYIKKQIE QYMSDTPCPK CKGTRLKPEA
     LAVTVGGKNI FEFANMSIKE ELEFINNLKL SEKNTIIANQ ILKEIKSRLQ FLIDVGLDYL
     DLNRKSGTLS GGESQRIRLA SQIGSGLVGV LYILDEPSIG LHQRDNDKLI STLQHLRDLG
     NTLVVVEHDE DTMKAADFIV DVGPGAGEHG GKIVAAGNIN EIKKCKESIT GQYLTGEKKI
     EVPRERRKGN NQFIEIIGAR ENNLKNINVK FPLGVLTSVT GVSGSGKSTL VNEILYKGLN
     KKINRSKMNP GLHKDILGVE NIDKVINIDQ SPIGRTPRSN PATYTGLFDV IRELFANTAE
     ARMRGYKSGR FSFNVKGGRC EACRGDGIIK IEMQFLSDVY VPCEVCKGKR YNRETLEVRY
     KGKNIDEVLN MTVEEALEFF SNIPRAKAKL QTLMDVGLGY LRLGQPSTQL SGGEAQRIKL
     AYELSKRSTG KTFYILDEPT TGLHIDDVNR LIQILQRLVD AGNTVVVIEH NLDVIKCSDY
     IIDLGPEGGD RGGTIIDCGT PEKISQNNNS YTGYYLKTKL
//
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