ID   UUP_BUCAI               Reviewed;         596 AA.
AC   P57445;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=BU364;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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}.
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; BA000003; BAB13068.1; -; Genomic_DNA.
DR   RefSeq; NP_240182.1; NC_002528.1.
DR   RefSeq; WP_010896086.1; NC_002528.1.
DR   AlphaFoldDB; P57445; -.
DR   SMR; P57445; -.
DR   STRING; 107806.10039034; -.
DR   EnsemblBacteria; BAB13068; BAB13068; BAB13068.
DR   KEGG; buc:BU364; -.
DR   PATRIC; fig|107806.10.peg.378; -.
DR   eggNOG; COG0488; Bacteria.
DR   HOGENOM; CLU_000604_36_0_6; -.
DR   OMA; AQADKMR; -.
DR   Proteomes; UP000001806; 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; 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   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; Cytoplasm; DNA damage; DNA repair; DNA-binding; Hydrolase;
KW   Nucleotide-binding; Reference proteome; Repeat.
FT   CHAIN           1..596
FT                   /note="ATP-binding protein Uup"
FT                   /id="PRO_0000093027"
FT   DOMAIN          1..222
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00848"
FT   DOMAIN          290..516
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00848"
FT   REGION          519..596
FT                   /note="C-terminal domain (CTD), binds DNA"
FT                   /evidence="ECO:0000250|UniProtKB:P43672"
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         322..329
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00848"
SQ   SEQUENCE   596 AA;  69392 MW;  77691AE68D2E6B98 CRC64;
     MSLINIHNAS LSFSNLQILE KSTFHINKNE RVCLIGKNGA GKSTLLKIIN KKQDLDEGQI
     IYKKNTTTAY LEQNNPKNLN ISIYDFIALG LKEHEKNKKK HTNEIVKIEK IIELIKLNKN
     TLLSHLSGGL LRKVALGRVL VREPDILLLD EPTNHLDMKT IKWLETFLKK FSGSILFVSH
     DRNFIQNVST RIIDLDRGKL VSWPGDYENF IKLKNESYRI EKIQKQLFDK NLEKEEQWIR
     KGIKARSTRN EGRVKKLKIL QKEQKDYKKI EKINNIEINQ SKNYLGKIIF KLDNIDFLVN
     NKIIIKNFSS IIQHGDKLAL IGDNGCGKST LIKIIIGENK PQKGKIYIGK GLKISYFDQN
     RSFLNPNKSI IENIDYGKEK ILLNSREQHI IRYLKNFLFK PNQLKSLVKT LSGGECNRLL
     LAQLFLKPSN VLILDEPTND LDLDTLQLLE KIIIAYKGTV IIVSHDKTFI KNTAKKCWFF
     EKNGFINTHF SQYDSLKKEK NNFHKEKIQK NKSKINLAIK IKNNFKKELN AILYEIETIE
     LDIKTLQKKV NEPDFFKKTL EEKLPTLKML AQKERKLGKK ILFWEKLEKN IINTKI