ID A0A1S8FME0_9BURK Unreviewed; 1033 AA.
AC A0A1S8FME0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=B0B52_02605 {ECO:0000313|EMBL:OOG46648.1};
OS Polaromonas sp. A23.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=1944133 {ECO:0000313|EMBL:OOG46648.1, ECO:0000313|Proteomes:UP000218978};
RN [1] {ECO:0000313|EMBL:OOG46648.1, ECO:0000313|Proteomes:UP000218978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A23 {ECO:0000313|EMBL:OOG46648.1,
RC ECO:0000313|Proteomes:UP000218978};
RA Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA Frostegard A.;
RT "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT isolation strategy.";
RL Submitted (FEB-2017) 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:OOG46648.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MUNO01000006; OOG46648.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S8FME0; -.
DR STRING; 1944133.B0B52_02605; -.
DR OrthoDB; 9809851at2; -.
DR Proteomes; UP000218978; 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}; Reference proteome {ECO:0000313|Proteomes:UP000218978};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00205};
KW SOS response {ECO:0000256|HAMAP-Rule:MF_00205};
KW 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 698..1030
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT ZN_FING 294..321
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT ZN_FING 833..859
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT BINDING 74..81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT BINDING 734..741
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ SEQUENCE 1033 AA; 113454 MW; 6638F67BF37F52CF CRC64;
MEGFAAPYTV NSPNDGKYLA STAAGGKQVA EPDQSRYLAQ ALAAQRISIR GARTHNLKNI
DLDIPRNQLV VITGLSGSGK SSLAFDTLYA EGQRRYVESL STYARQFLQL MDKPDVDMIE
GLSPAISIEQ KATSHNPRST VGTVTEIHDY LRLLFARAGT PFCPEHDLPL QAQSVSEMVD
HVLALPEDTK LMILAPVARE RKGEFIDVFA EMQAHGYVRF RVDGTAYEFD ELPKLKKAEK
HNIDVVIDRL KVRPDMQQRL AESFEAALRL ADGKALAMEM DSGKEHLFSA KFSCPVCSYS
LSEMEPRLFS FNSPVGACPS CDGLGHMEFF DPARVVAFPS LSLASGAVKG WDRRNGYYFS
MLESLAKHYK FDLDTAFENL PAEVQQVVLH GSGDEEIKFS YVMDSGNFAG KKINKKHPFE
GVITNFERRY RETDSAAVRE ELARYRSLQP CPDCEGTRLR NEARHVYLVS APQTDGTPGE
RKAIYEISSV TLRESFDYFN ALAMEGAKAE IAGKVVREIG LRLKFLNDVG LNYLSLDRSA
ETLSGGESQR IRLASQIGSG LTGVMYVLDE PSIGLHQRDN DRLIGTLKHL RDIGNSVLVV
EHDEDMIRAA DHVIDMGPGA GIHGGRVMAQ GSYADVVANP DSLTGKYLAQ ILKIAVPKRR
TPWLPTVVKA PYRDPKKPSK FAPSAAGIKR AAREAEHLRT QGDMQAIRVV NATGHNLKSV
SVDFPVGLLT CVTGVSGSGK STLVNDTLYA AVARTLYRAH EEPAPHESIE GIEHFDKVIN
VDQSPIGRTP RSNPATYTGL FTPIRELMAE MNTARERGYG PGRFSFNVAG GRCEACQGDG
VVKVEMHFLP DVYVPCDVCK GMRYNRETLE VQYKGKNIAQ VLDLTVEDAA EFFKAVPVIA
RKLHTLLDVG LSYIKLGQAA TTLSGGEAQR VKLALELSKR DTGRTLYILD EPTTGLHFAD
IDLLLKVLHQ LRDAGNTIVV IEHNLDVIKT ADWLIDMGPE GGAGGGSVVG VGTPEDIAAN
PDSHTGRYLK RLL
//
