ID F9GPM2_HAEHA Unreviewed; 647 AA.
AC F9GPM2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=GG9_1007 {ECO:0000313|EMBL:EGT75483.1};
OS Haemophilus haemolyticus M19501.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=1028803 {ECO:0000313|EMBL:EGT75483.1, ECO:0000313|Proteomes:UP000003258};
RN [1] {ECO:0000313|EMBL:EGT75483.1, ECO:0000313|Proteomes:UP000003258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M19501 {ECO:0000313|EMBL:EGT75483.1,
RC ECO:0000313|Proteomes:UP000003258};
RX PubMed=21952546; DOI=10.1128/JB.05863-11;
RA Jordan I.K., Conley A.B., Antonov I.V., Arthur R.A., Cook E.D.,
RA Cooper G.P., Jones B.L., Knipe K.M., Lee K.J., Liu X., Mitchell G.J.,
RA Pande P.R., Petit R.A., Qin S., Rajan V.N., Sarda S., Sebastian A.,
RA Tang S., Thapliyal R., Varghese N.J., Ye T., Katz L.S., Wang X., Rowe L.,
RA Frace M., Mayer L.W.;
RT "Genome Sequences for Five Strains of the Emerging Pathogen Haemophilus
RT haemolyticus.";
RL J. Bacteriol. 193:5879-5880(2011).
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: 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:EGT75483.1}.
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DR EMBL; AFQO01000008; EGT75483.1; -; Genomic_DNA.
DR RefSeq; WP_005631772.1; NZ_AFQO01000008.1.
DR AlphaFoldDB; F9GPM2; -.
DR PATRIC; fig|1028803.3.peg.1051; -.
DR eggNOG; COG0488; Bacteria.
DR Proteomes; UP000003258; 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; 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}; 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 544..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 578..639
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 647 AA; 73296 MW; 3E9E0BCF88D62019 CRC64;
MALISLTNGY LSFSDAPLLD HAELHIEPNE RVCLVGRNGA GKSTLLKIIA GDVLMDDGKI
QYEKDLVVSR LEQDPPRNAQ GNIFDYVAEG VGHLTDLLKE YHHISVQLEE NYSDQILSQL
EQVQAKLEHA DGWRFENKIN EVLLKLGLNP NTKLSALSGG WLRKAALARA LVCDPDVLLL
DEPTNHLDVE AIEWLENFLL DFQGSIVFIS HDRSFIRKMA TRIVDLDRGQ LVSYPGNYDL
YLTTKEENLR VEALQNELFD KRLAQEEVWI RQGIKARRTR NEGRVRALKA MREERRQRRD
VMGTAKLQLD TSSRSGKIVF EMEDVSYEIA GKTLLKDFST TILRGDKIAL VGPNGCGKTT
FIKLLLGEIQ PTSGKIRCGT KLDIAYFDQY RADLDPEKTV MDNVADGKQD IEVNGVKRHV
LGYLQDFLFP PKRAMTPVKA LSGGERNRLL LAKLLLKPNN LLILDEPTND LDVETLELLE
EILTDYQGTL LIVSHDRQFI DNTATECYLF EGEGLLNKYV GGFFDAKQQQ ANFWASKAVE
EQAKAKKSEP LKEESAVKND RTSKPKSVKL SYKEQRELEQ LPQLLEKLET KITVLQAEIA
DPAFFQQAHD ITDAKLKELA DTEAELETAF LRWEELEEKK NLTDGKA
//
