ID A0A0Q5DWQ6_9BURK Unreviewed; 635 AA.
AC A0A0Q5DWQ6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=ASF61_18325 {ECO:0000313|EMBL:KQQ46355.1};
OS Duganella sp. Leaf126.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1736266 {ECO:0000313|EMBL:KQQ46355.1, ECO:0000313|Proteomes:UP000051032};
RN [1] {ECO:0000313|EMBL:KQQ46355.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ46355.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ46355.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ46355.1};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQQ46355.1}.
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DR EMBL; LMNW01000002; KQQ46355.1; -; Genomic_DNA.
DR RefSeq; WP_056151368.1; NZ_LMNW01000002.1.
DR AlphaFoldDB; A0A0Q5DWQ6; -.
DR STRING; 1736266.ASF61_18325; -.
DR OrthoDB; 9762051at2; -.
DR Proteomes; UP000051032; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|HAMAP-Rule:MF_00848};
KW 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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00848}; Repeat {ECO:0000256|HAMAP-Rule:MF_00848};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 1..253
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 320..537
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 534..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 598..632
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
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 352..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
SQ SEQUENCE 635 AA; 70523 MW; 6387677BA3DE4AC4 CRC64;
MAVISLSSAQ LAFGHVALLD HAEFSLEAGE RVGLIGRNGT GKSSLLKIIS GRFKLDDGLL
VMQQNLQIAY VEQEPVFDPE MTVHDAVASG MGELPGLLKE YDALTGQFGQ GNDDAVMERM
HEIQVKLDAA DAWSLSNKVE TVLDRLNLTG DMLMKTLSGG MQKRVALARA LVSAPDVLLL
DEPTNHLDFT SIMWLEGLLR DFRGSVLFIT HDRSFLDNVA TRIIELDRGR LLSYPGNFTT
YQARKAEQLE NEEVENAKFD KFLAQEEVWI RKGVKARRVR DEGRVRRLEA LRLQRSARRE
QQGQVKLEVG AGERSGKIVA ELENVSKRFG DRVIVDNFTG TILRGDKVGL IGANGAGKTT
MLKMILGELA PDTGHAKLGT KLQVAYFDQM RTQLNEDASL IDTISPGSDW VEVNGQRKHS
MSYLNDFLFS PERARSPVKT LSGGERNRLL LARLFAKPAN CLVLDEPTND LDIDTLELLE
ELLEEYTGTV FLVSHDRTFL DNVVTQVIVA EGEGQWREFV GGYTDWERVR DTAASKPAAR
PAPVKAEAPA APAVAPSAKA KKLSFKEQRE LDELPKLIAA LEDEQTALNL QLSDADFYKK
NASEAKRVNA RVAEIEDELL AALEKWEQIE ARQRG
//
