ID G4FCE8_9GAMM Unreviewed; 638 AA.
AC G4FCE8;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-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=HAL1_20445 {ECO:0000313|EMBL:EHA13655.1};
OS Halomonas sp. HAL1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=550984 {ECO:0000313|EMBL:EHA13655.1, ECO:0000313|Proteomes:UP000005692};
RN [1] {ECO:0000313|EMBL:EHA13655.1, ECO:0000313|Proteomes:UP000005692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain {ECO:0000313|Proteomes:UP000005692};
RX PubMed=22156396; DOI=10.1128/JB.06359-11;
RA Lin Y., Fan H., Hao X., Johnstone L., Hu Y., Wei G., Alwathnani H.A.,
RA Wang G., Rensing C.;
RT "Draft Genome Sequence of Halomonas sp. Strain HAL1, a Moderately
RT Halophilic Arsenite-Oxidizing Bacterium Isolated from Gold-Mine Soil.";
RL J. Bacteriol. 194:199-200(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHA13655.1}.
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DR EMBL; AGIB01000095; EHA13655.1; -; Genomic_DNA.
DR RefSeq; WP_008959937.1; NZ_CP130610.1.
DR AlphaFoldDB; G4FCE8; -.
DR PATRIC; fig|550984.5.peg.3965; -.
DR Proteomes; UP000005692; 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: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 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..248
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 315..532
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 529..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 566..593
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 347..354
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
SQ SEQUENCE 638 AA; 71319 MW; 16E6BA3A576F4ADF CRC64;
MTLLRLEQLQ LAYGTHVLLN RADLTVEKGE RLALVGRNGT GKSTLLKLVA GDILPDDGSI
WRAPGLKIGV LAQELPESSG LTIFDMVAQG LPEAGELLSE YDHLINDPDP DMDRMATLQT
RLEAIDGWSY HQRIDTVLTR LGLPPEAEMS SLSGGWRRRV ALARALVAEP DLLLLDEPTN
HLDLDTIAWL EEQLLAFNGA VLLITHDRAF LSKLATNILE LDRGQLGRYP GKYEEYQARK
QHELEVEARE HAEFDKKLAQ EEAWIRQGVK ARRTRNEGRV RALEAMRNER SQRRERQGNA
NLTVDRGERT GKRVVELQGV TQRFGDDVIL RDINLEVLRG DRIGFLGRNG AGKTTLLKIL
LGELEPTEGK VQMGTNLKVA YFDQLRAGLE LDKTVYDNVA QGSDRVSVGG KDRHVMSYLQ
DFLFTPERVR QPVKALSGGE SNRLLLAKLF TQPANVLVLD EPTNDLDMET LELLEELLLD
FDGTLLLVSH DRTFMDNVVT SMLAFEGDGV VREYVGGYTD WIRQGGKLPP APWEGAARQR
TEPTSETPKK VTEAPAAPAK KSVKLSYNLQ RELDALPAEI ERLESEVESL ESEIGDPAFY
QQEAEAVTAK LHSLEKVQKA LEVAMERWME LEAMAGGE
//