ID S6GJR1_9GAMM Unreviewed; 630 AA.
AC S6GJR1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=OFPII_06730 {ECO:0000313|EMBL:EPJ48304.1};
OS Osedax symbiont Rs1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae.
OX NCBI_TaxID=1330036 {ECO:0000313|EMBL:EPJ48304.1, ECO:0000313|Proteomes:UP000014822};
RN [1] {ECO:0000313|EMBL:EPJ48304.1, ECO:0000313|Proteomes:UP000014822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rs1 {ECO:0000313|Proteomes:UP000014822};
RA Yi H., Goffredi S.;
RT "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT Osedax worms: functional variation and environmental selection.";
RL Submitted (MAY-2013) 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: 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:EPJ48304.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ASZJ01000038; EPJ48304.1; -; Genomic_DNA.
DR AlphaFoldDB; S6GJR1; -.
DR PATRIC; fig|1330036.3.peg.633; -.
DR Proteomes; UP000014822; 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}; Reference proteome {ECO:0000313|Proteomes:UP000014822};
KW Repeat {ECO:0000256|HAMAP-Rule:MF_00848}.
FT DOMAIN 4..249
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 316..534
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT COILED 570..624
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 348..355
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
SQ SEQUENCE 630 AA; 69986 MW; 7FCC2EE76800A9D9 CRC64;
MPLIRLEKAS VAFGSRPLLE KVDFLIDPGE RVGLVGLNGA GKSTLMKVVT KEVLLDGGEL
WVDPSCKISV LSQILPAADD RKVWDVVASG LGEAVRLRAA YDLLANNSDD ASMRKLEHLQ
HELEAVDGWM LEQRVERVLT RLKLDGDALM NSLSGGWRRR AALGAALVTE PDLLLLDEPT
NHLDISTIEW LEKQLLDFKG GLLFVSHDRA MVNSLSTRIV ELDRGTLTSF NGNYDSYIEQ
KEILLEHEAR HNALFDKRLA EEEVWIRQGV KARRTRNEGR VRALEKLRSE RTSRLDRQGK
ANFSFEEASK SGKLVASLEN VCISYAGKKV VDNLNLMVQR GDRIGLIGPN GSGKSTLLKL
ILGELQPDSG EVVMGTKVEV AYFDQLRGQL EPEKSVVDNI AGGREMIEIN GRNRHVISYL
NDFLFAPERA RTPVKALSGG ECNRVLLAKL FSLPANVLVL DEPTNDLDVE TLELLEEILL
EFKGTILLVS HDRSFLDNVV TSSLVFEGDG RISPYVGGYK DWLRQRPAPS KVKTSAKNAP
VDASINTAKV KAAAVEPVKK KLSYKLQIEL KELPKKLEQA EAQVEKFQAQ TLAADFYQGE
HSVVSKALED LATAEQLVEG LMERWVVLEE
//
