ID W8L2I4_9GAMM Unreviewed; 630 AA.
AC W8L2I4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=M911_01775 {ECO:0000313|EMBL:AHK78125.1};
OS Ectothiorhodospira haloalkaliphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Ectothiorhodospira.
OX NCBI_TaxID=421628 {ECO:0000313|EMBL:AHK78125.1, ECO:0000313|Proteomes:UP000019442};
RN [1] {ECO:0000313|EMBL:AHK78125.1, ECO:0000313|Proteomes:UP000019442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A {ECO:0000313|EMBL:AHK78125.1,
RC ECO:0000313|Proteomes:UP000019442};
RX PubMed=25057327; DOI=10.7150/jgen.9123;
RA Singh K.S., Kirksey J., Hoff W.D., Deole R.;
RT "Draft Genome Sequence of the Extremely Halophilic Phototrophic Purple
RT Sulfur Bacterium Halorhodospira halochloris.";
RL J Genomics 2:118-120(2014).
RN [2] {ECO:0000313|Proteomes:UP000019442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A {ECO:0000313|Proteomes:UP000019442};
RA Singh K.S.;
RT "Draft Genome Sequence of extremely halophilic bacteria Halorhodospira
RT halochloris.";
RL Submitted (FEB-2014) 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; CP007268; AHK78125.1; -; Genomic_DNA.
DR RefSeq; WP_025280457.1; NZ_JAJNQR010000002.1.
DR AlphaFoldDB; W8L2I4; -.
DR KEGG; hhc:M911_01775; -.
DR PATRIC; fig|1354791.3.peg.751; -.
DR HOGENOM; CLU_000604_36_0_6; -.
DR OrthoDB; 9808609at2; -.
DR Proteomes; UP000019442; 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; 1.
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:UP000019442};
KW Repeat {ECO:0000256|HAMAP-Rule:MF_00848}.
FT DOMAIN 4..253
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 320..537
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 538..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 568..622
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 352..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
SQ SEQUENCE 630 AA; 69774 MW; 5CB4B58293B226DE CRC64;
MPLLVMRNIQ LSYGHHPLLD GVDLTIEPGE RLCLVGRNGA GKSTLMRMLK GEIQADDGEI
VRSDGLKVAM LEQAVPKGVE GSVYDVVADG LGALGDTVRR YHGLIRAMET GADEAQLKAL
EQCQHELEAG DGWMLEQRVE MVLSRLGLEA DAPFHGLSGG LKRRVLLARA LVTGPDLLLL
DEPTNHLDVA AIEWLEEFLL GFEGTLLFIT HDRAFLRRLA TRIIELDRGR LTSWPGDYDT
YLTRKAEALE AEERQNALFD KKLAQEEVWI RQGIKARRTR NEGRVRALKA LRAERSERRE
RQGTARLQTR SAAPSGRIVA EAENVSFSFD GKPVIRDFSA LVMRGDKVGI LGPNGAGKTT
LLKLLLGQLE PQSGHIRLGT NLEVAYFDQH RAALDEEASV MDNVGEGRDR LTLGDESRHV
LSYLQDFLFE PARARQPVKA LSGGERNRLL LAKLFTRPAN VLVLDEPTND LDADTLEMLE
ARVVEFPGTV LVVSHDRDFL DNVATSVIAF EGEGCFREYV GGYSDWLRQR PKAKAPSATS
VAAPAAQAPK AKPAPKSAKL GYKDQRELDA LPKRIEALEA ELADIQQTLG DPDFYQRPKE
EIAAVQARME SLETELAQAY ERWETLESGG
//
