ID I3TKV7_TISMK Unreviewed; 963 AA.
AC I3TKV7;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
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:AFK53395.1};
GN OrderedLocusNames=TMO_1556 {ECO:0000313|EMBL:AFK53395.1};
OS Tistrella mobilis (strain KA081020-065).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC Geminicoccaceae; Tistrella.
OX NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK53395.1, ECO:0000313|Proteomes:UP000005258};
RN [1] {ECO:0000313|EMBL:AFK53395.1, ECO:0000313|Proteomes:UP000005258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK53395.1,
RC ECO:0000313|Proteomes:UP000005258};
RX PubMed=22458477; DOI=10.1021/ja301735a;
RA Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT agents.";
RL J. Am. Chem. Soc. 134:8625-8632(2012).
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; CP003236; AFK53395.1; -; Genomic_DNA.
DR AlphaFoldDB; I3TKV7; -.
DR STRING; 1110502.TMO_1556; -.
DR KEGG; tmo:TMO_1556; -.
DR PATRIC; fig|1110502.3.peg.1603; -.
DR eggNOG; COG0178; Bacteria.
DR HOGENOM; CLU_001370_0_2_5; -.
DR Proteomes; UP000005258; Chromosome.
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; 3.30.190.20; -; 1.
DR Gene3D; 1.10.8.280; ABC transporter ATPase domain-like; 1.
DR Gene3D; 1.20.1580.10; ABC transporter ATPase like domain; 3.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR HAMAP; MF_00205; UvrA; 1.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
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:UP000005258};
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 287..602
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 616..944
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT ZN_FING 747..773
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT BINDING 648..655
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ SEQUENCE 963 AA; 106086 MW; E5AE922470993D94 CRC64;
MVRDQMRDTT RLISVRGARE HNLKDVDVDI PRDRLVVITG LSGSGKSSLA FDTIYAEGQR
RYVESLSAYA RQFLELMQKP DVERIDGLSP AISIEQKTTS RNPRSTVGTV TEIYDYMRLL
WARVGIPYSP ATGLPIESQT VSQMVDRMME MGDGSRLLLL APVVRGRKGE YRKELAELMK
RGFTRVKIDG EIHEIEDAPA LDKKRKHDIE VVVDRIVIRE GLGNRLADSV ETALDLADGI
MIAENADTGD RTTFSARFAC PVSGFTIDEI EPRLFSFNNP YGACPDCDGL GVKSHFDPEL
VVPDPSLGLR DGAIAPWAKS TTQFYNQTLA GIAAHYKVTL TQSWEKLPDR VRQAILFGSG
EEAIKIRYED GARNYTVDRP FEGVIPNLER RWRETDSAFI REELSRFQGN RPCETCGGQR
LKDTALAVKI DMKNISEVTA LSIGEARSWF GALDGRLDAK RQEIAQRILK EINERLRFLT
EVGLDYLTLA RGSGSLSGGE SQRIRLASQI GSRLTGVLYV LDEPSIGLHQ RDNDRLLAAL
KDLRDLGNSV LVVEHDEDAI RAADHVIDMG PGAGEHGGKV VAEGTPAEIM ANPASLTGRY
LTGAKLIPVP EERRKGTGES ITLVGARSNN LHDVTASFPL GTFTCVTGVS GGGKSTLVIE
TLYQAIARRL NGARTHPGQH DRIDGLEHID KIINIDQSPI GRTPRSNPAT YVGLFTQIRD
WFAGLPEAKA RGYKPGRFSF NVKGGRCEAC QGDGVIRIEM HFLPDVYVQC DACKGKRYNR
ETLEVQFKGK SIADVLDMTV DEGLDFFQAM PSIREKLRTI AEVGLGYIRL GQSATTLSGG
EAQRVKLAKE LSRRATGRTL YILDEPTTGL HFDDVRKLLE VLHTLVDQGN TVVVIEHNLD
VIKTADWLID MGPEGGSGGG RIVAEGTPED VIHNPASHTG HYLGRHLAME DAKRGGNQII
SAE
//
