ID A0A1H1BTW0_9GAMM Unreviewed; 626 AA.
AC A0A1H1BTW0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=ATP-binding protein Uup {ECO:0000256|HAMAP-Rule:MF_00848};
DE EC=3.6.1.- {ECO:0000256|HAMAP-Rule:MF_00848};
GN Name=uup {ECO:0000256|HAMAP-Rule:MF_00848};
GN ORFNames=SAMN05216569_1558 {ECO:0000313|EMBL:SDQ55375.1};
OS Pseudoxanthomonas sp. CF125.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1855303 {ECO:0000313|EMBL:SDQ55375.1, ECO:0000313|Proteomes:UP000199049};
RN [1] {ECO:0000313|EMBL:SDQ55375.1, ECO:0000313|Proteomes:UP000199049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF125 {ECO:0000313|EMBL:SDQ55375.1,
RC ECO:0000313|Proteomes:UP000199049};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-
CC Rule:MF_00848};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00848}.
CC Note=Associates with ribosomes. {ECO:0000256|HAMAP-Rule:MF_00848}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC Uup subfamily. {ECO:0000256|HAMAP-Rule:MF_00848}.
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DR EMBL; FNLD01000001; SDQ55375.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1BTW0; -.
DR STRING; 1855303.SAMN05216569_1558; -.
DR OrthoDB; 9808609at2; -.
DR Proteomes; UP000199049; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00848}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00848};
KW DNA damage {ECO:0000256|HAMAP-Rule:MF_00848};
KW DNA repair {ECO:0000256|HAMAP-Rule:MF_00848};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00848};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00848};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00848}; Reference proteome {ECO:0000313|Proteomes:UP000199049};
KW Repeat {ECO:0000256|HAMAP-Rule:MF_00848}.
FT DOMAIN 4..246
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 313..530
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
FT BINDING 345..352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
SQ SEQUENCE 626 AA; 69835 MW; 1AD6E50B88B02900 CRC64;
MSLMQLQRVD FSIGGPLLLE HVDLTLEPNE RVCIVGRNGA GKSTLMRLLA GEITPDDGEV
RLQNGVVVAR MAQEVPQDTS GTVFDVVAEG LGDLGHLLAL YHHALHDGDM EAMGDAQEKI
EAQHGWDLDL RVQQVLTKLE LPEDADFAAL SGGMKRRVLL AQALVRKPDI LLLDEPTNHL
DIDAIAWLEG FLKQFEGSIV FVTHDRSFLR ALATRIVEID RGQVTSWPGD YENYLRRREE
RLHAEAQENA RFDKLLAQEE IWIRQGIKAR RTRNEGRVTA LKALRRERSQ RRDLSGNVRM
EVSAAQNSGK KVIEFEHVTQ AYDGRVLLND VSATIMRGDR VGIIGPNGAG KSTLLKIMLG
ELQPQQGEVR LGTGLQVAYF DQHRSQLNDS LNALENVAEG RDFIEINGTR KHIIGYLQDF
LFSPERARAP ITRLSGGERN RLLLAKLFAQ PSNLLVMDEP TNDLDVETLE LLEELLGEYK
GTLLLVSHDR EFIDNVVTST LVLEGQGRLA DYVGGYTDWV RQRPSALFNA ESAAPVKASP
SPVQTAAAAT AAAPKRKLSY KDARELELLP ERIEKLEAEI AARADAMNEP KFYQQDSATI
LAYNEASAKL QAELEHAYQR WNELDA
//
