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Database: UniProt
Entry: A0A1G6WUD9_9PROT
LinkDB: A0A1G6WUD9_9PROT
Original site: A0A1G6WUD9_9PROT 
ID   A0A1G6WUD9_9PROT        Unreviewed;       956 AA.
AC   A0A1G6WUD9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-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=SAMN05421720_101255 {ECO:0000313|EMBL:SDD68807.1};
OS   Rhodospira trueperi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospira.
OX   NCBI_TaxID=69960 {ECO:0000313|EMBL:SDD68807.1, ECO:0000313|Proteomes:UP000199412};
RN   [1] {ECO:0000313|EMBL:SDD68807.1, ECO:0000313|Proteomes:UP000199412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700224 {ECO:0000313|EMBL:SDD68807.1,
RC   ECO:0000313|Proteomes:UP000199412};
RA   de Groot N.N.;
RL   Submitted (OCT-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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00205}.
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DR   EMBL; FNAP01000001; SDD68807.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6WUD9; -.
DR   STRING; 69960.SAMN05421720_101255; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000199412; 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; 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; 2.
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:UP000199412};
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          364..600
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          605..942
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   ZN_FING         745..771
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         36..43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         646..653
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   956 AA;  104547 MW;  4F43D5288E968D66 CRC64;
     MTPPATHTIR VTGAREHNLK GIDVTLPRDR LVVITGLSGS GKSSLAFDTI YAEGQRRYVE
     SLSAYARQFL ELMQKPDVES IEGLSPAISI EQKTTSRNPR STVGTVTEIH DYMRLLWARV
     GVPHSPATGL PIESQTVSQM VDAIMAMGEG TRLYLLAPII RGRKGEYRKE LGELRKRGFQ
     RVKVDGEVHD IADVPALDKK RKHDIAVVVD RVIVKSGLET RLADSVETAL GLSDGLLITE
     DASSGEETVF SAKFACPVSG FTIEEIEPRL FSFNNPFGAC PACDGLGVKL YFDPDLVVPN
     PDKTLRDGAI APWSSYGQPA PYYAQALASV ATHYGGDMDT PWRDMPERAR EVLLHGSGDE
     IIALHFDDGS RSYRTEKPFE GVIPNIARRW RETESAGMRE ELSRYQASHP CESCEGFRLK
     PEALAVKIDS RHIGEISDLS ISAALDWFAG LEERLRPKDR EIAHRILREI NERLGFLTSV
     GLTYLTLSRT SGTLSGGESQ RIRLASQIGS GLTGVLYVLD EPSIGLHQRD NDRLLATLKR
     LRDLGNTVIV VEHDEDAIRA ADHLVDMGPG AGVHGGTIVA EGTPEEVMAN PASLTGQYLT
     GGRTVTVPDD RRPGNGKALR IEGARGNNLQ DLTVDIPLGT FTCVTGVSGG GKSTLIVETL
     YKALARHLHG ARELPAPHDA IKGVEHIDKI VDIDQSPIGR TPRSNPATYT GAFTPIRDWF
     ANLPDAKARG YKPGRFSFNV KGGRCEACQG DGVIKIEMHF LPDVYVTCDV CKGKRYNRET
     LEILFRGKSI ADVLDMTVEE AAEVFKAVPV IRDKMELLQR VGLGYVHLGQ QATTLSGGEA
     QRVKLAKELS RRATGRTLYI LDEPTTGLHF EDVRKLLEVL HHIVDQGNTV LVIEHNLEVI
     KTADHIIDLG PEGGSGGGRL VAQGTPEAVA ETRESYTGQY LKGHLLEAAA RKRRPA
//
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