ID A0A1U9NPH5_9BACT Unreviewed; 633 AA.
AC A0A1U9NPH5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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 ECO:0000313|EMBL:AQT69510.1};
GN ORFNames=STSP2_02701 {ECO:0000313|EMBL:AQT69510.1};
OS Anaerohalosphaera lusitana.
OC Bacteria; Planctomycetota; Phycisphaerae; Sedimentisphaerales;
OC Anaerohalosphaeraceae; Anaerohalosphaera.
OX NCBI_TaxID=1936003 {ECO:0000313|EMBL:AQT69510.1, ECO:0000313|Proteomes:UP000189674};
RN [1] {ECO:0000313|Proteomes:UP000189674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST-NAGAB-D1 {ECO:0000313|Proteomes:UP000189674};
RA Spring S., Bunk B., Sproer C.;
RT "Comparative genomics and description of representatives of a novel lineage
RT of planctomycetes thriving in anoxic sediments.";
RL Submitted (FEB-2017) 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; CP019791; AQT69510.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9NPH5; -.
DR STRING; 1936003.STSP2_02701; -.
DR KEGG; alus:STSP2_02701; -.
DR OrthoDB; 9760950at2; -.
DR Proteomes; UP000189674; 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}; 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:UP000189674};
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..538
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 529..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 353..360
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
SQ SEQUENCE 633 AA; 71782 MW; FDDFEFEC78B9CB52 CRC64;
MALLTLQNVS IGFGGPNILD DITLHVEQGE RLCLLGRNGA GKSTLLKLIN GTIKPTQGAI
QLEPGTKVAM LSQEVTGEGS HSVFDEVLIG LGELGHLLAE YELITSQVAH DPSAENMSRL
EKAQHKVDTN NAWSIHRQVQ TVLTHLDLNG SDTFGSLSAG TKRRVEMAKA LITKPDILLL
DEPTNHLDIN SITWLEGFLN DYPGTIVFVT HDRSLIRNLS TRIIDVELGT ISSWSCDYDT
FTQRKEQHTN ALLKHRAEFD KKLAEEEQWI RQGVRERRKR NQGRVRELQE MREQRRNRRQ
LAAKANIETQ QADLSGRLVI ETFKASFQYD HNPPIVDDLS TTILRGDKVG IIGPNGCGKT
TLLRLLLGQL SPTSGRVKLG TNLQIAYFDQ LHRQLDPDKA VWQNVIDGYE TVEFNGRKRH
VIGYLQDFLF MPEQSKKPVR TLSGGERNRL LLAQLFAKPT NLLVLDEPTN DLDMETLELL
EELLVNFQGT FLLVSHDREF LNNVVTSTLV FEGGGMVKEY AGGYDDWLKQ RKPLPQDETS
RPAKPEKKQK KSKPKPAQKK KLSYREKQEL EQLPARIEEL ESEQAGLHED MAKPDFYKQD
SEKISAVMNR SEKLDSKLAE LYERWEQLEE LNT
//
