ID A0A1K1P6M8_RUMFL Unreviewed; 940 AA.
AC A0A1K1P6M8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=SAMN02910280_2461 {ECO:0000313|EMBL:SFW42342.1};
OS Ruminococcus flavefaciens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=1265 {ECO:0000313|EMBL:SFW42342.1, ECO:0000313|Proteomes:UP000183461};
RN [1] {ECO:0000313|EMBL:SFW42342.1, ECO:0000313|Proteomes:UP000183461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YL228 {ECO:0000313|EMBL:SFW42342.1,
RC ECO:0000313|Proteomes:UP000183461};
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; FPIP01000007; SFW42342.1; -; Genomic_DNA.
DR RefSeq; WP_072300699.1; NZ_FPIP01000007.1.
DR AlphaFoldDB; A0A1K1P6M8; -.
DR Proteomes; UP000183461; 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; 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};
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 596..936
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT ZN_FING 251..278
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT ZN_FING 739..765
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 640..647
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ SEQUENCE 940 AA; 103710 MW; FFC810AF1ED62AD3 CRC64;
MTDKIIIKGA RANNLKNIDL ELPRDRLIVM TGLSGSGKSS LAFDTIYADG QRRYVESLSS
YARMFLGQME KPDVDSIEGL SPAISIDQKT TSKNPRSTVG TVTEIYDYLR LLYARIGVPH
CPVCGREISQ QTIDQMVDTL MELPVGTKLQ LLAPIVRNRK GQYSKELESA RKSGFVRARV
DGIMYELSED IKLDKNKKHN IDIIVDRIVI KEGIESRITD SLETVFNLTG GLAIADVIDG
EEILFSQNYA CPEHNISIGE LEPVMFSFNN PVGACPKCTG LGVFRHIDPD LIIPNKDLSI
EEGAINASGW NSLDETSIAT MYYRAISKKY GVPIDVPVKK LKKEQLDLFL YGTGDETLEL
KRPASLGGGT YNSPFEGVVN NLERRYKETS SEWSKNEIEE YMSEVECPVC KGKRLRDEYL
AVTVGDKNIS ELTDFSVKDG LGFFNGLKLS EHDSYVGERI IKEIKERLGF LKSVGLEYLT
LSRSSGTLSG GESQRIRLAT QIGSSLVGVL YILDEPSIGL HQRDNDKLIA TLKRLRDLGN
TLIVVEHDDD TMLAADYIVD IGPGAGIHGG EVVFAGTVDK LLKCKTSITG QYLSGRKKID
IPKKRRSGNG KFLTVRGAAE HNLQNIDVSI PLGELVCVTG VSGSGKSSLV NEIIYKYLAA
KLNRAKTRCG QFREMEGLEH LDKVICIDQS PIGRTPRSNP ATYTGVFSDI RDLFSKTPDA
KAHGYTSGRF SFNVKGGRCE ACEGDGIIKI EMHFLPDIYV PCEVCKGKRY NRETLDIHYK
GKSIYDVLEM TVDEGVEFFE HIPKIAKKLK TLQEVGLGYI KIGQPATTLS GGEAQRVKLS
TELSKRSTGN TIYILDEPTT GLHTADVHKL IDVLQRLTDQ GNTVLVIEHN LNVIKVADHI
IDLGPEGGDG GGTIVAQGTP EEVAQCEKSY TGQYLKGYLK
//