ID A0A3Q9G843_9GAMM Unreviewed; 639 AA.
AC A0A3Q9G843;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=EKO29_07540 {ECO:0000313|EMBL:AZQ83887.1};
OS Colwellia sp. Arc7-635.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=2497879 {ECO:0000313|EMBL:AZQ83887.1, ECO:0000313|Proteomes:UP000286937};
RN [1] {ECO:0000313|EMBL:AZQ83887.1, ECO:0000313|Proteomes:UP000286937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Arc7-635 {ECO:0000313|EMBL:AZQ83887.1,
RC ECO:0000313|Proteomes:UP000286937};
RA Lin J.;
RT "Complete Genome Sequences of Colwellia sp. Arc7-635, a Denitrifying
RT Bacterium Isolated from Arctic Seawater.";
RL Submitted (DEC-2018) 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; CP034660; AZQ83887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3Q9G843; -.
DR KEGG; cov:EKO29_07540; -.
DR OrthoDB; 9808609at2; -.
DR Proteomes; UP000286937; 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; 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}; Repeat {ECO:0000256|HAMAP-Rule:MF_00848}.
FT DOMAIN 1..253
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 320..567
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 551..574
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 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 639 AA; 71854 MW; 940016E4257A12A7 CRC64;
MELIRISQGE LAFGEDKVLD KADLSVQTGE RICLVGRNGA GKSTLMKVLM GLQVLDDGQV
LKSSTMQVAM LEQDPPESSD ISVFDYIAQG VKENADLIKR YHVIIHDVTE DPSESNLNKL
ANVQEQLELA NAWQDEQRIE QVMTTLALNP DDQICDLSGG WLRKVALAKA LVTAPDILLL
DEPTNHLDIK SVLWLESFLK DFAGTILFIS HDRAFIRGVS TRILDLDRGI LKSYPGNYDL
YIEQKAHDLQ VESQQNSLFD KKLAEEEVWI RQGVKARRTR NEGRVRALEK LRGERQARRE
VRNQSTMNIT QGDRSGKLVF EAEQVSIAFD DKVIIKSLDL LITRNDRLAF IGANGTGKST
LIKMIMGNLE ATSGKMRSGV NLDVAYFDQH RDALDVNQTV QEIVGEGKQE VMVNGKPRHV
LGYLQDFLFS PKRARTPVRA LSGGEKNRLL LARLFLRPSN LLILDEPTND LDIETLELLE
EVVANYAGTV ILVSHDRDFV NNCVNTCLYF DGTGHITQIV GGYDDVDDYL AHKDKQREAM
SKDVVKTAAK GTEEVESKAS KPANTQANKK RSFKEKKELE DLPGLIDELE TLIDELQQQV
NNADFFSQNQ EQSNKILNQL AKSESKLEVA YARWQELDD
//
