ID I2JMX1_9GAMM Unreviewed; 631 AA.
AC I2JMX1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=DOK_04367 {ECO:0000313|EMBL:EIF44323.1};
OS gamma proteobacterium BDW918.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae.
OX NCBI_TaxID=1168065 {ECO:0000313|EMBL:EIF44323.1, ECO:0000313|Proteomes:UP000003473};
RN [1] {ECO:0000313|EMBL:EIF44323.1, ECO:0000313|Proteomes:UP000003473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BDW918 {ECO:0000313|EMBL:EIF44323.1,
RC ECO:0000313|Proteomes:UP000003473};
RX PubMed=22740675; DOI=10.1128/JB.00678-12;
RA Kim S.M., Cho S.J., Lee S.B.;
RT "Genome Sequence of the Unclassified Marine Gammaproteobacterium BDW918.";
RL J. Bacteriol. 194:3753-3754(2012).
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:EIF44323.1}.
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DR EMBL; AJMK01000021; EIF44323.1; -; Genomic_DNA.
DR AlphaFoldDB; I2JMX1; -.
DR PATRIC; fig|1168065.3.peg.918; -.
DR eggNOG; COG0488; Bacteria.
DR HOGENOM; CLU_000604_36_0_6; -.
DR OrthoDB; 9762051at2; -.
DR Proteomes; UP000003473; 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:SF1; ABC TRANSPORTER; 1.
DR PANTHER; PTHR42855; ABC TRANSPORTER ATP-BINDING SUBUNIT; 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:UP000003473};
KW Repeat {ECO:0000256|HAMAP-Rule:MF_00848}.
FT DOMAIN 4..251
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 318..536
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 533..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..553
FT /note="Polar residues"
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 350..357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
SQ SEQUENCE 631 AA; 69968 MW; 2D94293D8FB2AD6F CRC64;
MPLLRATQLQ HSIGQQIVLD NAELQLEAGD RVCLLGRNGC GKSTLLRIVE GSAAVDAGEV
WRQPGVKIAR MEQTLDFASP DETIYDVVAD GLAGLGKVLR RYHELIIGDM GDAELKELEH
LQREIETNDG WSFQQRIDNI LTRLELDADA KVCSMSGGWR RRVALARALV CDPDILLLDE
PTNHLDLDGI LWLEQCVMSF QGCVLFVTHD RALIEKLATR IVELDRGILT NYDTNYTRYL
ELREHALEIE AEHNALFDKR LAQEEVWIRQ GIKARRTRNE GRVRALERMR SERSRRRVQS
GSANLSVNQA DRTGKVVAEL TDVSFSVPGK LLVDNLSLLV CRGDKLALIG PNGAGKTTLL
RLILGELEAQ SGTVKAGTNL QVAYFDQLRD RLDESQRVVD IVGQGRDAVT INGKDRHIMS
YLGDFLFSPE RARSHFGVLS GGERARVQLA CLFSQPANVL VMDEPTNDLD METLELLESL
LVDFSGTVLL VSHDRSFVDS VASSCLLFEG QGVISEHIGG YSEVSSYMSR RLAQQKAAPA
NPSPSSSAQA VATPKASPKA RKLSYKDQRE LDGLPSKIEN LELSLEKLAE KSGSAGFYQQ
DPSVIAEVLD KITATQAELD HCMERWLELA E
//