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Database: UniProt
Entry: A0A3A3FYD8_9BURK
LinkDB: A0A3A3FYD8_9BURK
Original site: A0A3A3FYD8_9BURK 
ID   A0A3A3FYD8_9BURK        Unreviewed;       950 AA.
AC   A0A3A3FYD8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
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:RJF99688.1};
GN   ORFNames=D3871_15030 {ECO:0000313|EMBL:RJF99688.1};
OS   Noviherbaspirillum saxi.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Noviherbaspirillum.
OX   NCBI_TaxID=2320863 {ECO:0000313|EMBL:RJF99688.1, ECO:0000313|Proteomes:UP000265955};
RN   [1] {ECO:0000313|Proteomes:UP000265955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K1R23-30 {ECO:0000313|Proteomes:UP000265955};
RA   Zhu H.;
RL   Submitted (SEP-2018) 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:RJF99688.1}.
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DR   EMBL; QYUO01000001; RJF99688.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A3FYD8; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000265955; 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:UP000265955};
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          603..944
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   ZN_FING         257..284
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   ZN_FING         747..773
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         31..38
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   950 AA;  105209 MW;  B9DA73CDC6CD0A59 CRC64;
     MEEIRIRGAR THNLKNINLE LPRNQLIVIT GLSGSGKSSL AFDTLYAEGQ RRYVESLSAY
     ARQFLQLMEK PDVDLIEGLS PAISIEQKAT SHNPRSTVGT VTEIHDYLRL LYARVGTPYC
     PDHPENALAA QSVSQMVDAV LAMPEDTKLM ILAPVVANRK GEHVDLFEAM QAQGFVRFRI
     QSGTHTARIY EIDDLPKLKK TEKHTIDVVI DRIKVKADVK QRLAESFETA LRLAEGRAIA
     LEMDSGKEHL YSNKFACNTC GYSLQELEPR LFSFNNPMGA CPECDGLGHI EFFDPKRIVA
     FPNLSLASGA VKGWDRRNQF YFQMLSNLAE HYNFDVDTPF EKLADSAQQV VLYGSGRQTV
     PFTYVNERGR AVVREHTFEG VVNNLQRRYR ETDSMAVKEE LAKFINQKQC PTCDGARLRV
     EARYVKVGNG KQERSIYEIA STPLRETLEF FEKLKLTGAK KEIADRIIKE IVSRLKFLNN
     VGLDYLSLER SADTLSGGEA QRIRLASQIG SGLTGVMYVL DEPSIGLHQR DNDRLIATLK
     HLRDIGNSVL VVEHDEDAIR CADYVVDMGI GAGVHGGEVI ARGPLQDILK SKKSLTAKYL
     NGTLAINVPK KRTAADPERQ LMITGASGNN LRNVSLELPV GLLTCVTGVS GSGKSTLIND
     TLHHAAARHL YGSQAEPSPY ESISGLEHFD KVIAVDQAPI GRTPRSNPAT YTGVFTPIRD
     LFSTVPMAKE RGYSAGRFSF NVKGGRCEAC QGDGVLKVEM HFLPDVYVPC DVCHGKRYNR
     ETLEVHYKGK SIHEVLEMTV EEAHEFFKPV PVVARKLQTL LDVGLGYIRL GQSATTLSGG
     EAQRVKLSLE LSKRDTGRTL YILDEPTTGL HFHDIDLLLK VIHRLRDQGN TVVIIEHNLD
     VIKTADWIVD LGPEGGAGGG QIIASGTPEV VAKTAASFTG KYLAPMLKKK
//
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