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Database: UniProt
Entry: F4GTT4_PUSST
LinkDB: F4GTT4_PUSST
Original site: F4GTT4_PUSST 
ID   F4GTT4_PUSST            Unreviewed;       599 AA.
AC   F4GTT4;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 63.
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   OrderedLocusNames=PT7_0003 {ECO:0000313|EMBL:AEC18543.1};
OS   Pusillimonas sp. (strain T7-7).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Pusillimonas.
OX   NCBI_TaxID=1007105 {ECO:0000313|EMBL:AEC18543.1, ECO:0000313|Proteomes:UP000008737};
RN   [1] {ECO:0000313|EMBL:AEC18543.1, ECO:0000313|Proteomes:UP000008737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T7-7 {ECO:0000313|EMBL:AEC18543.1,
RC   ECO:0000313|Proteomes:UP000008737};
RX   PubMed=21622753; DOI=10.1128/JB.05242-11;
RA   Cao B., Ma T., Ren Y., Ren Y., Li G., Li P., Guo X., Ding P., Feng L.;
RT   "Complete genome sequence of Pusillimonas sp. T7-7, a cold-tolerant diesel
RT   oil-degrading bacterium isolated from the Bohai Sea in China.";
RL   J. Bacteriol. 193:4021-4022(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=T7-7;
RA   Cao B., Ma T., Li P., Jiang L., Li Y., Guo X., Feng L.;
RT   "Genome Announcement Complete Genome Sequence of Pusillimonas sp. T7-7, a
RT   novel species isolated from the Bohai Sea, China.";
RL   Submitted (APR-2011) 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; CP002663; AEC18543.1; -; Genomic_DNA.
DR   RefSeq; WP_013741092.1; NC_015458.1.
DR   AlphaFoldDB; F4GTT4; -.
DR   STRING; 1007105.PT7_0003; -.
DR   KEGG; put:PT7_0003; -.
DR   eggNOG; COG0488; Bacteria.
DR   HOGENOM; CLU_000604_36_0_4; -.
DR   OMA; AQADKMR; -.
DR   OrthoDB; 9762051at2; -.
DR   Proteomes; UP000008737; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   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   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00848}; Repeat {ECO:0000256|HAMAP-Rule:MF_00848};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          7..220
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          287..506
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          499..522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          568..595
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
FT   COMPBIAS        502..522
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         39..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
FT   BINDING         319..326
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
SQ   SEQUENCE   599 AA;  67220 MW;  D6A766004C55C91C CRC64;
     MAATTLITLS NAQLAYGHHP LLDHTDFAIQ PGERIGLIGR NGAGKSSLLK VLDGRTLLDD
     GDLMRLGGLK IATVEQEPDL DNSLSIFETL CPDTSESEDW ARPSRVQALL EKLGLNPDDR
     IDGLSGGNRK RVALARALAD EPDLLLLDEP TNHLDFIGIA WLENLLLNTS CSVVIITHDR
     RFLDVVATRI VELDRGKLFS FPGNFTQWQQ RKTEWLEAEK QQNAKFDKVL AQEEAWIRQG
     VEARRTRNEG RVRRLEELRR ERISRRERQG NVNLAVAEGQ RSGKLVAELE HVTHRYGDKT
     IIHDLSTAIL RKDRIGLIGP NGAGKTTLLK VILGKLQPSS GTVRLGVNLT VGYFDQMRAQ
     LDENATLIDT INPGSEWVEI GDQRKHVMSY LEDFLFSPAR AHSPVQSLSG GERARLVLAR
     MFARPTNVLV LDEPTNDLDI ETLELLEELL QNYPGTVLLV SHDREFLNNV VTQTLAAEGN
     GHWQEYVGGY DEWLAQRPAQ PDTGEEKSRK KDAPAERPKP IRKSRITSWE LTELEGIPNA
     IAELESEQSG LASRLADGSL YRDAPDEVDA INQQLHVLEE KLNELFARWE MLEEKKNDS
//
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