ID A0A1T0A6Z2_9GAMM Unreviewed; 651 AA.
AC A0A1T0A6Z2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=B0181_02805 {ECO:0000313|EMBL:OOR91506.1}, NCTC10293_02004
GN {ECO:0000313|EMBL:STZ14410.1};
OS Moraxella caviae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=34060 {ECO:0000313|EMBL:OOR91506.1, ECO:0000313|Proteomes:UP000190435};
RN [1] {ECO:0000313|EMBL:OOR91506.1, ECO:0000313|Proteomes:UP000190435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 355 {ECO:0000313|EMBL:OOR91506.1,
RC ECO:0000313|Proteomes:UP000190435};
RA Engstrom-Jakobsson H., Salva-Serra F., Thorell K., Gonzales-Siles L.,
RA Karlsson R., Boulund F., Engstrand L., Moore E.;
RT "Draft genome sequence of Moraxella caviae CCUG 355 type strain.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:STZ14410.1, ECO:0000313|Proteomes:UP000255279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10293 {ECO:0000313|EMBL:STZ14410.1,
RC ECO:0000313|Proteomes:UP000255279};
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; MUXU01000021; OOR91506.1; -; Genomic_DNA.
DR EMBL; UGQE01000004; STZ14410.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T0A6Z2; -.
DR STRING; 34060.B0181_02805; -.
DR OrthoDB; 9808609at2; -.
DR Proteomes; UP000190435; Unassembled WGS sequence.
DR Proteomes; UP000255279; 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; 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:UP000190435};
KW Repeat {ECO:0000256|HAMAP-Rule:MF_00848}.
FT DOMAIN 4..251
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 323..541
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 539..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..584
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 355..362
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
SQ SEQUENCE 651 AA; 71616 MW; DE46FFACA24D1F08 CRC64;
MSLITLKNIH LAFGVAPILD GVDFSLAAGE RVCLIGRNGE GKSTLMKLIA GTAVADSGEV
LIAGSTKVAM LAQDVPSDDG TLLDVVMAGG GDTAELLRQY YTLSERCGAG DMAACDDMAA
LQHEIDARHG WGLERKARAL LDNMGLDPEA KLAELSGGRK RRALLARALV ADPDVLLLDE
PTNHLDVESI DWLENYLLNQ NLSLLFITHD RQFVDNLATR IVELDRGKLS SYDVSQGTGG
YARYQELKAQ ELAAEAKAFA DFDKKLAQEE VWIRQGIKAR RTRNEGRVRA LKALREERKA
RRDVVGNVSL TQQAAEKSGK IVCEVNHLTL KYAGKTLVKD FSTLLLRGDK VGIIGQNGVG
KTTLIRTILG LDDGAKTDGT VRLGTSINVA FFDQLKDQLD GEKSVADNVS EGSDYVEVNG
RKTHILGYLQ DFLFTPNRAR TPIKALSGGE KARVLLARLL LQPANVLVLD EPTNDLDMAT
LELLEEYVVN FDGTVLLISH DRTFMDNVVT QTWVFDTDKN GDGVVQEYVG GYQDYLVQKS
RQTPAPKPKA EKTEKADKAQ KADDTKNATN DKPKPEKRKL SYKEQRELEA LPDEISALET
EQAELSEALA DGSLFVSDLA LATQHSERLA QIDELLLEKL ERWDWLESQG K
//