UUP_BUCAP
ID UUP_BUCAP Reviewed; 592 AA.
AC Q8K9I3;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=ATP-binding protein Uup {ECO:0000255|HAMAP-Rule:MF_00848};
DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_00848};
GN Name=uup {ECO:0000255|HAMAP-Rule:MF_00848}; OrderedLocusNames=BUsg_352;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
RN [2]
RP DISCUSSION OF SEQUENCE, AND FAMILY.
RX PubMed=30597160; DOI=10.1016/j.jmb.2018.12.013;
RA Murina V., Kasari M., Takada H., Hinnu M., Saha C.K., Grimshaw J.W.,
RA Seki T., Reith M., Putrins M., Tenson T., Strahl H., Hauryliuk V.,
RA Atkinson G.C.;
RT "ABCF ATPases involved in protein synthesis, ribosome assembly and
RT antibiotic resistance: structural and functional diversification across the
RT tree of life.";
RL J. Mol. Biol. 431:3568-3590(2019).
CC -!- FUNCTION: Probably plays a role in ribosome assembly or function. May
CC be involved in resolution of branched DNA intermediates that result
CC from template switching in postreplication gaps. Binds DNA and has
CC ATPase activity. {ECO:0000255|HAMAP-Rule:MF_00848}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00848};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00848}.
CC Note=Associates with ribosomes. {ECO:0000255|HAMAP-Rule:MF_00848}.
CC -!- DOMAIN: The C-terminal domain (CTD) helps bind DNA.
CC {ECO:0000250|UniProtKB:P43672}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC Uup subfamily. {ECO:0000255|HAMAP-Rule:MF_00848}.
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DR EMBL; AE013218; AAM67905.1; -; Genomic_DNA.
DR RefSeq; WP_011053872.1; NC_004061.1.
DR AlphaFoldDB; Q8K9I3; -.
DR SMR; Q8K9I3; -.
DR STRING; 198804.BUsg_352; -.
DR EnsemblBacteria; AAM67905; AAM67905; BUsg_352.
DR KEGG; bas:BUsg_352; -.
DR eggNOG; COG0488; Bacteria.
DR HOGENOM; CLU_000604_36_0_6; -.
DR OMA; AQADKMR; -.
DR OrthoDB; 1112046at2; -.
DR Proteomes; UP000000416; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.380; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00848; Uup; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR032781; ABC_tran_Xtn.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR043686; Uup.
DR InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF12848; ABC_tran_Xtn; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Cytoplasm; DNA damage; DNA repair; DNA-binding;
KW Hydrolase; Nucleotide-binding; Repeat.
FT CHAIN 1..592
FT /note="ATP-binding protein Uup"
FT /id="PRO_0000093028"
FT DOMAIN 1..221
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00848"
FT DOMAIN 289..516
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00848"
FT REGION 518..592
FT /note="C-terminal domain (CTD), binds DNA"
FT /evidence="ECO:0000250|UniProtKB:P43672"
FT COILED 516..550
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00848"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00848"
FT BINDING 321..328
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00848"
SQ SEQUENCE 592 AA; 68733 MW; 0CBFA9AD1F5CD861 CRC64;
MPLISIQNAF LAFSDLEILK NAVLYINKKE RISLIGKNGA GKSTLLKVIN KNQELDHGSI
IYQKNIKISY LKQDNPKNLD ISIYDFIKNQ LKKENNKEIN INTIVEIKKI IKTFQIDKHS
LLSELSGGSL RKVVLGSALL SQPDVLLLDE PTNHLDINTI AWLEKFLKKF SGTTLFISHD
RSFIQNLCTR IIDLDRGKLT SFPGDYKEFI KLKKENNRIE KTKKKLFDQH LEKEEIWIRK
GIKARTTRNE GRVRNLKVLR KEYKNYKKIE NFNNVIINEI KNYSGKIIFK LKNISFFIEK
KTIIQSFSSI IQYGDKIGLI GNNGSGKSTM IKILMGEKKI QKGSIHFGTK LNIAYFDQDR
STLDSNKSIL ENVNNGREKI VLNGKEQHLI GYLKKFLFKP NQMKCLVKNL SGGECNRLLL
AKLFLKPSNV LILDEPTNDL DLDTLELLEN IIIKYSGTVL IVSHDRNFIE NTVNKYWIFK
GDGLINTHFS SHNNIIKEKN KKIQKKYVLN PIKSNISFLK TKQNQVKKEL KKVLNEIEKI
ENSIKTLKIQ MNEPDFFKQH IKNQLPIVKQ FNIEEKKLEK ILIYWENLEK KL
