ID Q6MRC9_BDEBA Unreviewed; 982 AA.
AC Q6MRC9;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 134.
DE RecName: Full=UvrABC system protein A {ECO:0000256|ARBA:ARBA00039316};
DE AltName: Full=Excinuclease ABC subunit A {ECO:0000256|ARBA:ARBA00042156};
GN Name=uvrA {ECO:0000313|EMBL:CAE77829.1};
GN OrderedLocusNames=Bd0159 {ECO:0000313|EMBL:CAE77829.1};
OS Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS HD100).
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=264462 {ECO:0000313|EMBL:CAE77829.1, ECO:0000313|Proteomes:UP000008080};
RN [1] {ECO:0000313|EMBL:CAE77829.1, ECO:0000313|Proteomes:UP000008080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100
RC {ECO:0000313|Proteomes:UP000008080};
RX PubMed=14752164; DOI=10.1126/science.1093027;
RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA Schuster S.C.;
RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT genomic perspective.";
RL Science 303:689-692(2004).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA family.
CC {ECO:0000256|ARBA:ARBA00038000}.
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DR EMBL; BX842646; CAE77829.1; -; Genomic_DNA.
DR RefSeq; WP_011162770.1; NC_005363.1.
DR AlphaFoldDB; Q6MRC9; -.
DR STRING; 264462.Bd0159; -.
DR KEGG; bba:Bd0159; -.
DR eggNOG; COG0178; Bacteria.
DR HOGENOM; CLU_001370_0_2_7; -.
DR Proteomes; UP000008080; 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-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
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 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 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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA excision {ECO:0000256|ARBA:ARBA00022769};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Excision nuclease {ECO:0000256|ARBA:ARBA00022881};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008080};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 638..967
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 982 AA; 109019 MW; 84D2DBEAA92CC3E1 CRC64;
MKDIHLWGVK QNNLKNIEVK IPVGSMTVIC GPSGSGKSSL AFETLFAEGQ RRFIESMSNY
ARQFLNKAPK PDIEGINNIP PAISIEQKNT VKSSRSTVGT TTEIIDYLRL LYEKIGKSYC
PTHHCPTEKE SVTEATDKVL KNFAGKRGYL LVEINSEGRV AEGKKLHSLL LQDGYLRIYI
PKVTEVKKPA AKAAGKKTKA SGKKASKKVE TPEIVATHPG GLTNEEMGTV VEIGEAAAIK
KGLPKETFYL VIDRMSFNED ERGRLADSLT QAYEASIKYN THLITRRATI LSTDGERLQV
SEEASCPVCG YTPPPLSSKL FSFNSPIGAC PTCKGFGNIL DIDEEKVIPN PNLSLAQGAL
SPFWMPSAAH EKKQLLAYCK KTKIDTHTPW KDLPKAERDV IWNGNKDFFG VRGLFEYLDQ
IKYKMHVRVF ISRFRSPFQC PTCKGARLRT EANHVLIANS NINDLSNLTI EDLNTFFQKL
EVTPFQQEVA GEVLKQIRSR LEFLMRVGVH YLSLGRETRT LSGGEYQRLI LANQLGMGLS
QALYVLDEPT VGLHPRDNDR LISILKDLKD LGNTLVIVEH DHDVIKASEH IIEMGPGSGY
LGGEVVYSGT TEKFYDYEKS NTVPFLKPSK NWQALRTIRP VDVDNYKVKI ELKGAKGHNL
KNLDVTFPLN RLVTVTGVSG SGKSTLISKT LYPALARALD IEYMPAQDYS GLDGVEHIKN
VLLIDQSPIG KSARSSPITY LKAFDAIRMI MSTTPESQSR GYTAGTFSLN VDGGRCPACK
GTGYEEIDMM FMDNVVIPCD VCDGKKYRPE ILEIQYKNKN IHEILSMTVN EAMNFFVAHP
NIRKPLSVLK EVGLDYLQLG QPANSLSGGE SQRLKIAKEL SQVQQKSTLY ILDEPTTGLH
FREVELLMKV LNKLIETGGS VVVVEHNLDV IRGSDYVIDL GPEAGKKGGN IVATGTPDDI
MKVKKSLTGQ YLKRYIESHQ TS
//