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Database: UniProt
Entry: A0A212RSZ2_9PROT
LinkDB: A0A212RSZ2_9PROT
Original site: A0A212RSZ2_9PROT 
ID   A0A212RSZ2_9PROT        Unreviewed;       603 AA.
AC   A0A212RSZ2;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=SAMN07250955_11411 {ECO:0000313|EMBL:SNB75787.1};
OS   Arboricoccus pini.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Geminicoccaceae; Arboricoccus.
OX   NCBI_TaxID=1963835 {ECO:0000313|EMBL:SNB75787.1, ECO:0000313|Proteomes:UP000197065};
RN   [1] {ECO:0000313|EMBL:SNB75787.1, ECO:0000313|Proteomes:UP000197065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B29T1 {ECO:0000313|EMBL:SNB75787.1,
RC   ECO:0000313|Proteomes:UP000197065};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-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; FYEH01000014; SNB75787.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A212RSZ2; -.
DR   OrthoDB; 9762369at2; -.
DR   Proteomes; UP000197065; 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; 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   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:UP000197065};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_00848}.
FT   DOMAIN          6..216
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          283..503
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   BINDING         38..45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
FT   BINDING         315..322
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
SQ   SEQUENCE   603 AA;  66325 MW;  138D9178ABD5D055 CRC64;
     MAPPLFILKD VHLTFGGTPL LEGAELTVSA GQKLALVGRN GSGKSTFLKI AAAIIEPDRG
     DRALQQGVTL RYLPQEPDLR GFATTGDYVV AGLTSGDDPH RASYLLQQLG LTGLEEPARL
     SGGEARRAAL ARAMAPEPDI LLLDEPTNHL DLPAIEWLEG ELKRSRSALV LISHDRRFLE
     TLSDSVLWLD RGRTRLLAKG FAAFEAWRDD ILELEEKERH RLDRKIAQEQ DWLRYGVTAR
     RKRNMGRLRA LQGLRKERRE QRRVLGQVEM TAAEGPSSGK LVIEAKGVAK SYDDRPIVQP
     LSLRLKKGDR LGVVGPNGAG KTTLLNLLTG ALAPDAGTVR LGANVVMVTL DQKREALDPE
     TSLQDTLTGG RGDHVFVGGQ PRHVMGYMKD FLFSAEQART PVRVLSGGER GRLMLARALA
     APSNLLVLDE PTNDLDLETL DLLEELLADY EGTVLVVSHD RDFLDRVATS VLAFEGAGNW
     TEYAGGYSDM ITQRGHGVLA REPLEARRPD KGQAAAREAA APRRRLGFKE QHALKTLPEE
     IERRRREIAA LEAKLADPAL FAADPALFAR TTEALTATHD ALAEAEDRWL ELEMLREELE
     GQA
//
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