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Database: UniProt
Entry: A0A368KYS0_9BURK
LinkDB: A0A368KYS0_9BURK
Original site: A0A368KYS0_9BURK 
ID   A0A368KYS0_9BURK        Unreviewed;       940 AA.
AC   A0A368KYS0;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=DU000_11375 {ECO:0000313|EMBL:RCS56560.1};
OS   Parvibium lacunae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Parvibium.
OX   NCBI_TaxID=1888893 {ECO:0000313|EMBL:RCS56560.1, ECO:0000313|Proteomes:UP000252357};
RN   [1] {ECO:0000313|EMBL:RCS56560.1, ECO:0000313|Proteomes:UP000252357}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMB9 {ECO:0000313|EMBL:RCS56560.1,
RC   ECO:0000313|Proteomes:UP000252357};
RX   PubMed=29498621; DOI=10.1099/ijsem.0.002667;
RA   Chen W.M., Xie P.B., Hsu M.Y., Sheu S.Y.;
RT   "Parvibium lacunae gen. nov., sp. nov., a new member of the family
RT   Alcaligenaceae isolated from a freshwater pond.";
RL   Int. J. Syst. Evol. Microbiol. 68:1291-1299(2018).
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:RCS56560.1}.
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DR   EMBL; QPGB01000006; RCS56560.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A368KYS0; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000252357; 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:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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}; Membrane {ECO:0000256|ARBA:ARBA00023136};
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:UP000252357};
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}; Translocase {ECO:0000256|ARBA:ARBA00022967};
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          604..936
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         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;  104479 MW;  B6B833661E6BB188 CRC64;
     MNTEIKVRGA RTHNLKNINL DIPRDQLVVI TGLSGSGKSS LAFDTLYAEG QRRYVESLSA
     YARQFLQLME KPDVDLIEGL SPAISIEQKA TSHNPRSTVG TVTEIHDYLR LLYARVGTPY
     CPDHPEQSLE AQTVSEMVDH VLALPEGTKL MVMAPVVRER KGEFVDLFAN MQAQGFVRFR
     VDGQIVEADN LPKLKKTEKH NIDVVVDRLK LNPEFKQRLA ESFENALRLA EGRALALEMD
     SDKEHLFSSK FACPICSYSL QELEPRLFSF NNPMGACPTC DGLGQVQFFD PKRVVQFPNL
     SLGSGAIKGW DRRNQFYYQM LTSLANHYEF DLDSPFEKLP DNIQHLVLYG SGKEKVPFAY
     VGERGKTVIR EHAFEGILPN LERRYKETDS MAVREELAKY INSKPCPDCH GTRLRKEARF
     VKVASEPIYA ISAWPLRNAL EFFTDIRLKG AKAAIAEKII QEIRSRLQFL NNVGLDYLCL
     ERSADTLSGG EAQRIRLASQ IGSGLTGVMY VLDEPSIGLH QRDNDRLIGT LKHLRDLGNS
     VLVVEHDEDM IRAADYVVDM GLGAGEHGGC VIAQGTPKEV QKAKGSITGQ FLRGERGIHV
     PEERRQPDPE KQLVITGASG NNLKNVTLNL PVGLLTCVTG VSGSGKSTLI NDTLYHAVAQ
     HLYNSSTEPA PFEEISGLEH FDKVINVDQS PIGRTPRSNP ATYTGLFTPI RELFAGVSTA
     RERGYEAGRF SFNVKGGRCE ACQGDGVIKV EMHFLPDVYV PCDVCHGKRY NRETLEVQYK
     GKNIHQVLEM TVEQAHEFFN AVPSIKRKLQ TLLDVGLGYI RLGQSATTLS GGEAQRVKLA
     LELSKRDTGR TLYILDEPTT GLHFHDIELL LKVIHTLRDH GNTLVIIEHN LDVIKTADWL
     IDLGPEGGAG GGQILVEGPP EKIAASKQSF TGQYLGPLLK
//
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