ID A0A381EDM2_9GAMM Unreviewed; 635 AA.
AC A0A381EDM2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=NCTC13294_02180 {ECO:0000313|EMBL:SUX24979.1};
OS Cardiobacterium valvarum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC Cardiobacteriaceae; Cardiobacterium.
OX NCBI_TaxID=194702 {ECO:0000313|EMBL:SUX24979.1, ECO:0000313|Proteomes:UP000254572};
RN [1] {ECO:0000313|EMBL:SUX24979.1, ECO:0000313|Proteomes:UP000254572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13294 {ECO:0000313|EMBL:SUX24979.1,
RC ECO:0000313|Proteomes:UP000254572};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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; UFUW01000001; SUX24979.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A381EDM2; -.
DR OrthoDB; 9762051at2; -.
DR Proteomes; UP000254572; 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; 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}; 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:UP000254572};
KW Repeat {ECO:0000256|HAMAP-Rule:MF_00848}.
FT DOMAIN 5..250
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 317..535
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT COILED 572..633
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
FT BINDING 350..357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
SQ SEQUENCE 635 AA; 70489 MW; FBA1164EB6C7C2C3 CRC64;
MPLLLTAQDL SLAFGWRPLL DHVNFSLESG ERVALLGRNG EGKSTLLNVL RGAQTPDDGS
LRISEGVRIA YLPQDPPAAD ARTVREVVRD GLAETAALVE RYQTLLAAHD AHDADELARL
EAAVAAADGW QLDNRIDGIL QRFDLDGTTQ MADLSGGWRR RVWLARVLVA RPDVLLLDEP
TNHLDMGTII WLENLLNNFA SAVVFVTHDR AFLEKVANRI WELDRGRLLD VKSDYRRFLR
TREEAQHAEA EAQARFDKKL AEEEIWIRQG IKARRTRNEG RVRALKAMRA ERAARIERQG
KANLQLDAGE RSGRQVIVAE NLSFAHAGGA PLVQDFSDII ERGEKIGLVG ANGAGKTTLL
RLLLGELPPT AGRLKHGTKL EVAYFDQLRA QLDPEETLRD SVGAGRDYIE TNGQRKHIAA
YLQDFLFPPE RWRTPVSALS GGERARLLLA RLFAQPANVL VLDEPTNDLD IETLELLEEV
LADYPGTVLL VSHDRAFLDA VVTRLWVFNR HKGKIEQIVG GFSDWLQQGG DIAQLEEAAA
PAVKTAEKPV APAAPPAEKR GNKLSYKYQR ELEALPAQIE AAEAEVARLT AAVQEADFYQ
QPQEAQQAGF AALEAAQQQL DALVERWMQL EDGEV
//
