ID A0A0K6GVL2_9GAMM Unreviewed; 635 AA.
AC A0A0K6GVL2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=Ga0061064_0213 {ECO:0000313|EMBL:CUA82776.1};
OS Pseudidiomarina woesei.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Pseudidiomarina.
OX NCBI_TaxID=1381080 {ECO:0000313|EMBL:CUA82776.1, ECO:0000313|Proteomes:UP000182598};
RN [1] {ECO:0000313|Proteomes:UP000182598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27808 {ECO:0000313|Proteomes:UP000182598};
RA Varghese N.;
RL Submitted (AUG-2015) 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; CYHB01000001; CUA82776.1; -; Genomic_DNA.
DR RefSeq; WP_055437935.1; NZ_LIPW01000001.1.
DR AlphaFoldDB; A0A0K6GVL2; -.
DR OrthoDB; 9808609at2; -.
DR Proteomes; UP000182598; 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; 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}; Coiled coil {ECO:0000256|HAMAP-Rule:MF_00848};
KW 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 4..254
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 321..547
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT COILED 569..599
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
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 353..360
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
SQ SEQUENCE 635 AA; 71212 MW; 6281E5ECFF82C7F0 CRC64;
MNLVRLHQAQ LAFGNYPILD HADLVIESGE RVCIVGRNGA GKSTLLKIIA GEVLLDDGAV
QVVGDTVVAR LPQDPPANSD QSVYDFVAEG LAELGKLLQQ YHHVVQELNN EPSSQILMNR
MATLQTAIEA ANGWQIQSRI ESTLTQLELP EDTTMSSLSG GWLRRVALAR ALVVDPDLLL
LDEPTNHLDV EMVTWLENKV KEFRGAVLFI SHDRAFIRNL ATRIVDLDRG HLTSFPGNYD
QYLTLKQEQL EVEEAQNAEF DKKLAQEEAW IRQGVKARRT RNEGRVRALQ DLRRQRQARR
EQQGSAKLAV QEANRSGKLV FEGEHLNLTF GDKTILRDFS LNLQRGDKVA LVGPNGCGKS
TLIRVLLGQQ GVDNGHIKLG TNLEVAYFDQ HRAQLDPELS VAENIGDGKQ DVTYNGRTRH
ILSYLQDFLF SPKQARTPVK ALSGGERNRA LLAKLFLQPS NFLILDEPTN DLDIDTLELL
EQIIAEYQGT VILVSHDREF VDNTATSVLL FEGQGRITEI VGGFTEINHY LSQLQGTKPV
KAQSQSADKK VQTSATPKKK LSYKLQRELD MLPEQIAALE EEQEKLEQQA SAADFYQRDH
SETGPVLERL GAIEEELMTA LERWTELENL QQESR
//
