ID A0A1T4LMG5_9GAMM Unreviewed; 634 AA.
AC A0A1T4LMG5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SAMN02745674_00065 {ECO:0000313|EMBL:SJZ55718.1};
OS Lysobacter spongiicola DSM 21749.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1122188 {ECO:0000313|EMBL:SJZ55718.1, ECO:0000313|Proteomes:UP000190061};
RN [1] {ECO:0000313|EMBL:SJZ55718.1, ECO:0000313|Proteomes:UP000190061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21749 {ECO:0000313|EMBL:SJZ55718.1,
RC ECO:0000313|Proteomes:UP000190061};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUXP01000001; SJZ55718.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4LMG5; -.
DR STRING; 1122188.SAMN02745674_00065; -.
DR OrthoDB; 9808609at2; -.
DR Proteomes; UP000190061; 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:UP000190061};
KW Repeat {ECO:0000256|HAMAP-Rule:MF_00848}.
FT DOMAIN 4..248
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 315..534
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 535..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 347..354
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
SQ SEQUENCE 634 AA; 69752 MW; 2B2815370AAE31C1 CRC64;
MPLITLNNVD YSVGGPLLLE NVDFAVEPGE RVALIGRNGA GKSTLLKLLS GDIQPDDGEI
RREGGARIAR LEQEVPAGAG GDVFDVVAAG MGELGAWLAE FHHLSHAEEF DAEAMSAVQA
KIDAAQGWSA DQRVTETLDK LGLDGDAAFS GLSGGMKRRV LLARALVSAP DLLLLDEPTN
HLDIEAIDWL EAFLKSWQGA LIFVTHDRRF LRALATRIVE IDRGKLTSWP GDWANYERRR
EERLNAEAQE NARFDKMLAQ EEVWIRQGIK ARRTRDEGRV RRLEAMRNER AARRDRTGNV
RMEFAQAENS GKKVIEAKRV SFDYGGKALL DDISTTVFRG DRIGLIGPNG SGKTTLLKTL
LGDLQPTAGE VKIGSNLQIA YFDQYRAVLR EDWNAIENVA EGREFVEVGG KQKHVIGYLQ
DFLFTPDRAR APITRLSGGE RNRLLLAKLF AQPSNLLVMD EPTNDLDVET LELLEELLGE
YPGTLLLVSH DRDFLDNVVT STLVMEGHGQ VGEYVGGYSD WLRQRRVGPA TPEIAGRAAA
PSAAPASAAS TASPATPSAP KRKLSYKDAR ELERLPAAIE QLETQVAAMT TRMNEPEFYQ
QGADAIATHN AELAELQGRL EAAYARWAEL EDPA
//
