ID B5JVV0_9GAMM Unreviewed; 639 AA.
AC B5JVV0;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=GP5015_1745 {ECO:0000313|EMBL:EDY86271.1};
OS gamma proteobacterium HTCC5015.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=391615 {ECO:0000313|EMBL:EDY86271.1, ECO:0000313|Proteomes:UP000004692};
RN [1] {ECO:0000313|Proteomes:UP000004692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC5015 {ECO:0000313|Proteomes:UP000004692};
RX PubMed=20472792; DOI=10.1128/JB.00510-10;
RA Thrash J.C., Stingl U., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA Giovannoni S.J.;
RT "Genome sequence of the novel marine member of the Gammaproteobacteria
RT strain HTCC5015.";
RL J. Bacteriol. 192:3838-3839(2010).
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; DS990604; EDY86271.1; -; Genomic_DNA.
DR AlphaFoldDB; B5JVV0; -.
DR STRING; 391615.GP5015_1745; -.
DR eggNOG; COG0488; Bacteria.
DR HOGENOM; CLU_000604_36_0_6; -.
DR OrthoDB; 6130096at2; -.
DR Proteomes; UP000004692; 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}; Reference proteome {ECO:0000313|Proteomes:UP000004692};
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..543
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 532..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 579..633
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
FT COMPBIAS 534..562
FT /note="Polar residues"
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 351..358
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; 71687 MW; C9D8499BF9CE997C CRC64;
MPLLRIKQLQ LAYGPHTLLD RVDMQLDAGE RVCLIGRNGT GKSTLMKIIA GEIQADDGEI
EHAPTLKVAR LVQDVPTDVE GSLFDVVAQG LGDMGEWLKQ HAHAVQRLSA GDDSAMKDLE
RAQSHIEAGD GWQVNQHVET VLSRLSLDPE QNFEALSGGM KRRVLLAQAL VTQPDILLLD
EPTNHLDIDS IRWLEDFLAQ YEGTLVFITH DRAFLRRLAT RIIELDRGQL TSWPGSYDKY
LAGKQAALDA EEKANAEFDK KLAKEEAWIR QGIKARRTRN EGRVRALKQL RQERLQRRER
SGTASLKMSQ ADLSGKIVIE AEDIHYAWND QAIVQNFSTR IMRGDRIGIV GPNGSGKSTL
LRLLLDKLPP DSGTLKLGTK LEIAYFDQLR DALDLNKSVT DNIGEGRDML PLPDGPRHVM
SYLQDFLFSA ERARQPVRSL SGGERNRLLL AKLFTKAFNL LVLDEPTNDL DAETLELLED
RLMSYQGTLL LVSHDREFLD NVVTSTLVFE NDTINEYIGG YSDWLRQREP LDGESSKAAQ
NSLKKAPSNA AKPNSGTAEK SPSKSATKKK LSYKDQRELE SLPAKIETLE SELSQLQETL
ADPSFYQSDN DTISQAQNQL QQLESDLEHC FERWEALEG
//
