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Database: UniProt
Entry: A0A176U9R3_9FIRM
LinkDB: A0A176U9R3_9FIRM
Original site: A0A176U9R3_9FIRM 
ID   A0A176U9R3_9FIRM        Unreviewed;       943 AA.
AC   A0A176U9R3;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-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   ORFNames=HMPREF2738_00381 {ECO:0000313|EMBL:OAD89589.1};
OS   Clostridiales bacterium KLE1615.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales.
OX   NCBI_TaxID=1715004 {ECO:0000313|EMBL:OAD89589.1, ECO:0000313|Proteomes:UP000077212};
RN   [1] {ECO:0000313|EMBL:OAD89589.1, ECO:0000313|Proteomes:UP000077212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLE1615 {ECO:0000313|EMBL:OAD89589.1,
RC   ECO:0000313|Proteomes:UP000077212};
RA   Wen L., He K., Yang H.;
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:OAD89589.1}.
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DR   EMBL; LXPQ01000033; OAD89589.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176U9R3; -.
DR   PATRIC; fig|1715004.3.peg.378; -.
DR   Proteomes; UP000077212; 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; 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:UP000077212};
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          601..937
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   ZN_FING         253..280
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         34..41
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   943 AA;  104561 MW;  EEABB0743C35F9CD CRC64;
     MENKKFIRIR GAAENNLKHI DLDIPRDELV VLTGLSGSGK SSLAFDTIYA EGQRRYMESL
     SSYARQFLGQ MEKPNVESIE GLPPAISIDQ KSTNRNPRST VGTVTEIYDY FRLLYARIGI
     PHCPVCGRKI SRQTVDQMVD SLMALKERTK ILLLAPVVRG KKGRHEKVLE QARKSGYVRV
     RIDGSQYDLE EEIKLDKNIK HNIEIIVDRL VIKEGIEKRL ADSLENVLKL ADGLAFVDVV
     DGTPMTFSQN FSCPDCGISI DEIEPRSFSF NNPFGACPTC FGLGYKMEFD EQLMIPDQSL
     SIDQGAIIVP GWQSCTDEGS FTRAILNALA EEFHFTLDVP FESYSKEIHD ILIHGTNKSV
     KVRYKGQRGE GVYDIVFEGL IKNVERRYRE TGSEAIKAEY ETFMRITPCS TCKGMRLKRE
     SLAVTVADKN IYEVTNLSIR DLASFLSDLE LTKTQQLIGE QILKEIRARV QFLIDVGLDY
     LCLSRATGTL SGGEAQRIRL ATQIGSGLVG VAYILDEPSI GLHQRDNDKL LGTLKHLRDL
     GNSVIVVEHD EDTMRAADYV VDIGPGAGEH GGQVVAAGTA EELMKNPASI TGKYLSGELK
     IPVPNTRREP QGWLTVVGAK ENNLKNITVN FPKGVFTCVT GVSGSGKSSL VNSILYQALA
     KQLNRARTIP GAYKEIKGIE QFDKVINIDQ SPIGRTPRSN PATYTGVFDM IRDLFASTVD
     AKTRGYNKGR FSFNVKGGRC EACSGDGIVK IEMHFLPDVY VPCEVCKGKR YNRETLEVKY
     KGKSIYDVLN MTVEEALTFF ENVPSIYRKI ETLYQVGLSY IRLGQPSTTL SGGEAQRIKL
     ATELSRKSTG KTIYILDEPT TGLHFADVHK LTEMLQKLVE NGNTVIVIEH NLDVIKTADY
     IIDMGPEGGD GGGTVVAQGT PEEVAECPQS YTGYYVKRVI ANG
//
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