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Database: UniProt
Entry: I2JMX1_9GAMM
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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
//
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