ID A0A0R0E9J5_9GAMM Unreviewed; 625 AA.
AC A0A0R0E9J5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=ABB34_05360 {ECO:0000313|EMBL:KRG86910.1};
OS Stenotrophomonas daejeonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=659018 {ECO:0000313|EMBL:KRG86910.1, ECO:0000313|Proteomes:UP000050940};
RN [1] {ECO:0000313|EMBL:KRG86910.1, ECO:0000313|Proteomes:UP000050940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16244 {ECO:0000313|EMBL:KRG86910.1,
RC ECO:0000313|Proteomes:UP000050940};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-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:KRG86910.1}.
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DR EMBL; LDJP01000029; KRG86910.1; -; Genomic_DNA.
DR RefSeq; WP_057640226.1; NZ_LDJP01000029.1.
DR AlphaFoldDB; A0A0R0E9J5; -.
DR STRING; 659018.ABB34_05360; -.
DR PATRIC; fig|659018.3.peg.983; -.
DR OrthoDB; 9808609at2; -.
DR Proteomes; UP000050940; 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:UP000050940};
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..532
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 535..554
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 625 AA; 69493 MW; 5571E7C3DD9F23E3 CRC64;
MPLITLQNVD YSVGGPLLLE KTELSIDAGE RIALIGRNGA GKSTLMKLMA GELKPDDGEV
RVQQGVRVAR LEQEVPHGAA GSVFDVVADG LGELGHWLAE FHRLSHAEVF DGDAMGKVQA
RIDAADGWAL DQRVAETLTK LELDGDAEFG RLSGGMKRRV LLARALVAGP DVLLLDEPTN
HLDIEAIDWL EGFLKGWSGC VVFVTHDRRF LRALATRIVE IDRGQVTSWP GDWANYERRR
EERLNAQAQE NARFDKLLAQ EEVWIRQGIK ARRTRDEGRV RRLKAMRNER SQRRELGGNV
RLEAAGAENS GKKVIDIRNI SFAFGERVMV RDFETTILRG DRIGLVGPNG SGKTTLLKLL
LGELQPDSGE VRQGTNLQIA YFDQYRATLR EDWSAIENVA EGADFIDLNG KRKHVHAYLQ
DFLFTPERAR APITRLSGGE RNRLLLAKLF AQPSNLLVMD EPTNDLDVET LELLEELLGD
YTGTLLLVSH DRDFLDNVVT STLVMEGEGR VGEYIGGYSD WLRQRPQVAQ EVAAKAPEKP
VAAPAAEPQP AAAKRKLSYK DARELEQLPV KIEKLELDVE GLTSAMNDPA FYTRSSAEVT
AHTQQLAKAQ AELDAAYARW EELDG
//
