ID A0A0S3PZN0_9BRAD Unreviewed; 602 AA.
AC A0A0S3PZN0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-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 ECO:0000313|EMBL:BAT61347.1};
GN ORFNames=GJW-30_1_03904 {ECO:0000313|EMBL:BAT61347.1};
OS Variibacter gotjawalensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Variibacter.
OX NCBI_TaxID=1333996 {ECO:0000313|EMBL:BAT61347.1, ECO:0000313|Proteomes:UP000236884};
RN [1] {ECO:0000313|EMBL:BAT61347.1, ECO:0000313|Proteomes:UP000236884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GJW-30 {ECO:0000313|EMBL:BAT61347.1,
RC ECO:0000313|Proteomes:UP000236884};
RA Lee J.S.;
RT "Investigation of the bacterial diversity of lava forest soil.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in beta-(1-->2)glucan export. Transmembrane domains
CC (TMD) form a pore in the inner membrane and the ATP-binding domain
CC (NBD) is responsible for energy generation.
CC {ECO:0000256|ARBA:ARBA00024722}.
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; AP014946; BAT61347.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3PZN0; -.
DR KEGG; vgo:GJW-30_1_03904; -.
DR OrthoDB; 9808609at2; -.
DR Proteomes; UP000236884; 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; 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 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:UP000236884};
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 REGION 506..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 602 AA; 65500 MW; 74B1D81502F50768 CRC64;
MAPPLIQLKD IALTFGGTPL LSGAELSVSE GERVCLVGRN GSGKSTLLKI AAGTVEADKG
TRFVQPGATV RYLPQEVDFG DAATTLDYVR QGLGPTDDPY QATYLLEQLG LTGDEPTQNL
SGGEARRAAI ARALAPDPDI LLLDEPTNHL DLTTIEWLES ELASRRAALV LISHDRRFLT
SLSRATVWLD RGITRRIDRG FGDFEAWRDD VLAEEEREQH KLGRKIVDEE HWLRYGVSGR
RKRNVKRLAG LQTLREKRRT YRGSTGSVKL GASEADASGA LVLDADHIAK AFGERVIVSD
FSTRIQRGDR IGIVGPNGAG KTTLINLLIG TEPPDSGTVR LGANLEVATL DQRRARLDPN
ATVAEALTGG SSDQVTIGGV RKHVSGYMKD FLFAPEQART PVHALSGGER GRLMLAQALA
QPSNLLVLDE PTNDLDIETL DVLEEMLSDY AGTVLLISHD RDFLDRVVNG VIVPEGSGKW
LEYAGGYSDM LTQRGADVRR PAAAKVKTAD KAAAPAPSRA SPKSKLSFKD KHALETLPKE
MDAFRATIAA LQSELDDPQL FVKNRKRFDE ASAAIAAAHV LLATAEERWL ELEIMREELE
NG
//
