ID A0A149VTM0_9PROT Unreviewed; 605 AA.
AC A0A149VTM0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, 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:KXW56528.1};
GN ORFNames=FV185_04790 {ECO:0000313|EMBL:KXW56528.1};
OS Ferrovum sp. PN-J185.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Ferrovales; Ferrovaceae;
OC Ferrovum.
OX NCBI_TaxID=1356306 {ECO:0000313|EMBL:KXW56528.1, ECO:0000313|Proteomes:UP000075387};
RN [1] {ECO:0000313|EMBL:KXW56528.1, ECO:0000313|Proteomes:UP000075387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN-J185 {ECO:0000313|EMBL:KXW56528.1,
RC ECO:0000313|Proteomes:UP000075387};
RA Poehlein A., Ullrich S.R., Schloemann M., Muehling M., Daniel R.;
RT "Genome sequence of the acidophilic iron oxidising Ferrovum strain PN-
RT J185.";
RL Submitted (JAN-2016) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:KXW56528.1}.
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DR EMBL; LQZA01000001; KXW56528.1; -; Genomic_DNA.
DR RefSeq; WP_067493182.1; NZ_LQZA01000001.1.
DR AlphaFoldDB; A0A149VTM0; -.
DR STRING; 1356306.FV185_04790; -.
DR PATRIC; fig|1356306.3.peg.473; -.
DR InParanoid; A0A149VTM0; -.
DR OrthoDB; 9762051at2; -.
DR Proteomes; UP000075387; Unassembled WGS sequence.
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; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000075387};
KW Repeat {ECO:0000256|HAMAP-Rule:MF_00848}.
FT DOMAIN 4..217
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 284..501
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT COILED 565..592
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
FT BINDING 316..323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
SQ SEQUENCE 605 AA; 68557 MW; 2DBBCFBEE8A70339 CRC64;
MPLVTLRHLS LAFGHHALLD NVNLVIEERQ RIGLIGRNGG GKSSLLKIVL GTVLPDSGER
WLQPGLIVGY VAQEDHFDDH KTVLDVVTQA SLLHNEWAPT HRIDTLLHSI GFKGDETVTQ
LSGGWRKKLG IACALINDPQ LLVLDEPTNH LDIDAIEWLE NLLKEFRGSV VFVTHDRAFL
DHVATDIVEL DRGQLAHFGH SFATYQLRKQ ELLAVEESHQ AKFDKLLAQE EVWIRKGIEA
RRTRNEGRVR RLEALRVERS RRRDRVGSVQ LNLHEGDQSG ELVVELDKVK ISYENRLLID
SFSTRIQRGD RIGIIGPNGS GKTSLLKTLL GESQPEEGSV KLGTKIQVAY FDQLREQLDP
EATLIDTISP GSDFIEINGQ RKHRVSYLGD FLFPPERTRA KVKSLSGGER NRLLLARLFA
KPANVVVLDE PTNDLDMDTL EVLEELLSEY KGTLFLVSHD RAFLDNVVTQ VIVLDGKGQV
TENAGGYSDW LAYVNRSLKK TEDTANTVAT EKKHITQEVR DKPKNRPEKM TNRELQELEA
LPEKIDTLEK EQLTINERLS DPSLYVSQKD EVKQLQDRLA VLQHEIETCL QRWEVLEQKL
LRVNG
//
