ID A0A145WSV3_9GAMM Unreviewed; 634 AA.
AC A0A145WSV3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=AMD27_02140 {ECO:0000313|EMBL:AMW77806.1};
OS Acinetobacter sp. TGL-Y2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1407071 {ECO:0000313|EMBL:AMW77806.1, ECO:0000313|Proteomes:UP000076238};
RN [1] {ECO:0000313|Proteomes:UP000076238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TGL-Y2 {ECO:0000313|Proteomes:UP000076238};
RA Zhang G.;
RL Submitted (APR-2016) 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; CP015110; AMW77806.1; -; Genomic_DNA.
DR RefSeq; WP_067655710.1; NZ_CP015110.1.
DR AlphaFoldDB; A0A145WSV3; -.
DR STRING; 1407071.AMD27_02140; -.
DR KEGG; acv:AMD27_02140; -.
DR OrthoDB; 9762051at2; -.
DR Proteomes; UP000076238; Chromosome.
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; 1.
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:UP000076238};
KW Repeat {ECO:0000256|HAMAP-Rule:MF_00848}.
FT DOMAIN 4..252
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 319..538
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
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 634 AA; 70414 MW; 81DF4C6CF6BB1F79 CRC64;
MAYITLRDVQ LAFGGPSLLD GANFNLERGE RVCLIGRNGE GKSTLLKLIE GSLLPDRGEV
SLQNGITISM LAQDVPMDSG KVADIVADGA GEAATVLRAY HEASDACVLG DMEACDRMGE
LQHKLDQVDG WALETKVNSI LSKMGLDPDA DLADLSGGRK RRVLLARALL TQPDVLLLDE
PTNHLDVESI EWLEKFLLDQ NNLTLLFISH DRSFVDSIAT RIVELDRGTL RSYEGNYSRY
LELKAMQMEA EEKQNALFDK KLAEEEVWIR QGIKARRTRN EGRVRELKAL REESKARRSQ
QGKVNMGTQD ANRSGKLVFD IEKLSVAFGN NAPIIRDFSA LVLRGDRIGL VGDNGVGKTT
LIKAILGELE HTGSVKTGTQ LEVAYFDQLR NALDLEKSVK DNVSEGSDFV DVTGGRRHIY
SYLQDFLFSP ERARTPVKAL SGGERNRILL AKLLLKPSNL IVMDEPTNDL DMVTLELLEE
MLGSYKGTLL LISHDRAFMD NVVTSTWVFD GKGHIDEYVG GYQDYLEQRP DQTAVDQKSD
VKKALAKAEA TAAAAAPKKV KLSYKDQRAL EQLPVEMEAL EKEQADINAK LADGSLFISN
NDQAMKLSAR LSEIDEQLLE KLEQWEQLEE MSKG
//
