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Database: UniProt
Entry: A3QDY2_SHELP
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ID   A3QDY2_SHELP            Unreviewed;       639 AA.
AC   A3QDY2;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 105.
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=Shew_1814 {ECO:0000313|EMBL:ABO23680.1};
OS   Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=323850 {ECO:0000313|EMBL:ABO23680.1, ECO:0000313|Proteomes:UP000001558};
RN   [1] {ECO:0000313|EMBL:ABO23680.1, ECO:0000313|Proteomes:UP000001558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1088 / PV-4 {ECO:0000313|Proteomes:UP000001558};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA   Fredrickson J., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella loihica PV-4.";
RL   Submitted (MAR-2007) 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; CP000606; ABO23680.1; -; Genomic_DNA.
DR   RefSeq; WP_011865612.1; NC_009092.1.
DR   AlphaFoldDB; A3QDY2; -.
DR   STRING; 323850.Shew_1814; -.
DR   KEGG; slo:Shew_1814; -.
DR   eggNOG; COG0488; Bacteria.
DR   HOGENOM; CLU_000604_36_0_6; -.
DR   OrthoDB; 9808609at2; -.
DR   Proteomes; UP000001558; 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; 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:UP000001558};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_00848}.
FT   DOMAIN          4..256
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          323..542
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   COILED          570..638
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         355..362
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;  71939 MW;  9AFA69C5ED1C3EE6 CRC64;
     MSLVRINNGS LAYGYTPLLQ NADFTIEPGE RVCIVGRNGA GKSSLMKVIG GEVLLDDGEF
     NIANDVKVSR LQQDPPKAEQ GTVYAYISAG LQEVGEKLER YHQLSHDVAH VDAQEMERLL
     KQMERLQSDL DHLNGWQLDT RINQTCELLG LDADASLASL SGGWQRKVAL ARALVSEPDL
     LLLDEPTNHL DIDTIEWLEE FLLNYRGAIV FISHDRGFIQ RMATRIVDLD RGVVTSWPGD
     YQTYLDGKAE WLRVEEEKNA QFDKKLAEEE AWIRQGIKAR RTRNEGRVRA LKALRMERME
     RINRQGGAKM AVADTERSGK LVFDIKDLNY NLPDKNLVKN FTTSVMRGDR IALIGPNGCG
     KSTLIKLLIG QLAPQSGEVK VGTKLEVAYF DQYREALDPE KTVEDNVGEG KKTVTINGQD
     RHILSYLQDF LFSPMRARTP VKALSGGEKN RLLLARLLLR PANLIILDEP TNDLDIETLE
     LLESLLTDYQ GTLLLVSHDR AFIDNTVTSS WWFTGNGGWS EYVGGYQDAV SQGAKFYSEE
     PVAKDAVQPK VAEPVKRETK AAAKAEKKLS YKLQRELDAL PAKMEQLEAE IESLQAVINE
     PDFYTQAQDL VSSRLNELAE LEQELEVCFE RWEELEALK
//
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