ID UUP_HAEIN Reviewed; 647 AA.
AC Q57242; O05056;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 132.
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}; Synonyms=uup-A;
GN OrderedLocusNames=HI_1300;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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; L42023; AAC22945.1; -; Genomic_DNA.
DR PIR; E64170; E64170.
DR RefSeq; NP_439451.1; NC_000907.1.
DR AlphaFoldDB; Q57242; -.
DR SMR; Q57242; -.
DR STRING; 71421.HI_1300; -.
DR EnsemblBacteria; AAC22945; AAC22945; HI_1300.
DR KEGG; hin:HI_1300; -.
DR PATRIC; fig|71421.8.peg.1352; -.
DR eggNOG; COG0488; Bacteria.
DR HOGENOM; CLU_000604_36_0_6; -.
DR OrthoDB; 9762051at2; -.
DR PhylomeDB; Q57242; -.
DR BioCyc; HINF71421:G1GJ1-1325-MONOMER; -.
DR Proteomes; UP000000579; 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 CDD; cd03221; ABCF_EF-3; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.287.380; Valyl-tRNA synthetase, C-terminal domain; 1.
DR HAMAP; MF_00848; Uup; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR032524; ABC_tran_C.
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 PANTHER; PTHR42855; ABC TRANSPORTER ATP-BINDING SUBUNIT; 1.
DR PANTHER; PTHR42855:SF1; ABC TRANSPORTER DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF16326; ABC_tran_CTD; 1.
DR Pfam; PF12848; ABC_tran_Xtn; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
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..647
FT /note="ATP-binding protein Uup"
FT /id="PRO_0000093030"
FT DOMAIN 1..253
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00848"
FT DOMAIN 320..546
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00848"
FT REGION 545..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..647
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 352..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00848"
SQ SEQUENCE 647 AA; 73268 MW; 85C949B0C0CF2B1B CRC64;
MALISLTNGY LSFSDAPLLD HAELHIEPNE CVCLVGRNGA GKSTLLKIIA GDVLMDDGKI
QYEKDLVVSR LEQDPPRNAQ GNIFDYVAEG VGHLTDLLKE YHQISVQLEE NYSDQILSQL
EQVQAKLEHA DGWRFENKIN EVLLKLGLNP NTKLSALSGG WLRKAALARA LVCDPDVLLL
DEPTNHLDVE AIEWLENFLL DFQGSIVFIS HDRSFIRKMA TRIVDLDRGQ LVSYPGNYDL
YLTTKEENLR VEALQNELFD KRLAQEEVWI RQGIKARRTR NEGRVRALKV MREERRQRRD
VMGTAKLQLD TSSRSGKIVF EMEDVSYEIA GKTLLKDFST TILRGDKIAL VGPNGCGKTT
FIKLLLGEIQ PTSGKIRCGT KLEIAYFDQY RADLDPEKTV MDNVADGKQD IEINGVKRHV
LGYLQDFLFP PKRAMTPVKA LSGGERNRLL LAKLLLKPNN LLILDEPTND LDVETLELLE
EILTDYQGTL LIVSHDRQFI DNTATECYLF EGKGHLNKYV GGFFDAKQQQ ANFWASKAVE
EQAKAKKSEP LKEESAVKND RTSKPKSVKL SYKEQRELEQ LPQLLEELET KITVLQAEIA
DPAFFQQAHD ITDAKLKALA DTEAELETAF LRWEELEEKK NLVEGKA
//
