ID A0A0W0VYK4_9GAMM Unreviewed; 613 AA.
AC A0A0W0VYK4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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_2 {ECO:0000313|EMBL:KTD25042.1};
GN Synonyms=uup {ECO:0000256|HAMAP-Rule:MF_00848};
GN ORFNames=Lisr_1267 {ECO:0000313|EMBL:KTD25042.1};
OS Legionella israelensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=454 {ECO:0000313|EMBL:KTD25042.1, ECO:0000313|Proteomes:UP000054761};
RN [1] {ECO:0000313|EMBL:KTD25042.1, ECO:0000313|Proteomes:UP000054761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bercovier 4 {ECO:0000313|EMBL:KTD25042.1,
RC ECO:0000313|Proteomes:UP000054761};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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}.
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:KTD25042.1}.
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DR EMBL; LNYH01000063; KTD25042.1; -; Genomic_DNA.
DR RefSeq; WP_058501619.1; NZ_UGOE01000001.1.
DR AlphaFoldDB; A0A0W0VYK4; -.
DR STRING; 454.Lisr_1267; -.
DR PATRIC; fig|454.4.peg.1372; -.
DR OrthoDB; 9762051at2; -.
DR Proteomes; UP000054761; 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:UP000054761};
KW Repeat {ECO:0000256|HAMAP-Rule:MF_00848}.
FT DOMAIN 4..246
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 313..531
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT COILED 552..606
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 345..352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
SQ SEQUENCE 613 AA; 69666 MW; 2CF87F350533802C CRC64;
MSIISLHGVT LNLAGNCLLE KVDWAIEAQD RIALIGRNGA GKSSLLKLLQ GHLTIDGGQI
NRQSSLRVAG LSQEVPVSAN ESVYHFLVKS LGLTGEVMAE YYRLSAKGSL EELAECQQKM
DRLQAWDLLP RVDMMASRLA LDPAAKMVSL SGGMKRRALL AAALIAEPDL LLLDEPTNHL
DMAAIEWLES YLKSYRGSLL IVTHDREFLQ QVANKIVEID KGQLYSYKCD YETYLDRREA
RRLSEEKQQN LFDKKLADEE AWIRQGIKAR RTRNEGRVRA LKAMREQYKN RRAELGKVKS
MELDVKRSGQ LVLEAKHLHY KLDDRYLIKD FSLLLTRGAK IGIIGPNGCG KTTLIRLLLG
ELSPHSGEIR RGTALEIAYF DQLRCQLDEG QTLMQNVADR ADYVSINGQQ KHVATYLREF
LFPPEQFNQS ISTLSGGERN RLLLAKLFAK PVNLLVMDEP TNDLDIETLE LLETILMDYP
GTLLLISHDR AFINQVVTSV LVFEAEGCFR EYVGGYEDYL FEKKELKEKS VKPSVKPRNT
SVKLSFNEQR ELAQLPQKIE VLEKKIAALQ MKMAEPQFYQ QDPQDISQYN QQLAADESEL
AVLYERWENL EAK
//
