ID F2G7K1_ALTMD Unreviewed; 363 AA.
AC F2G7K1;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE RecName: Full=Ribosome-binding ATPase YchF {ECO:0000256|HAMAP-Rule:MF_00944};
GN Name=ychF {ECO:0000256|HAMAP-Rule:MF_00944,
GN ECO:0000313|EMBL:AEA97651.1};
GN OrderedLocusNames=MADE_1007555 {ECO:0000313|EMBL:AEA97651.1};
OS Alteromonas mediterranea (strain DSM 17117 / CIP 110805 / LMG 28347 / Deep
OS ecotype).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=1774373 {ECO:0000313|EMBL:AEA97651.1, ECO:0000313|Proteomes:UP000001870};
RN [1] {ECO:0000313|EMBL:AEA97651.1, ECO:0000313|Proteomes:UP000001870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17117 / CIP 110805 / LMG 28347 / Deep ecotype
RC {ECO:0000313|Proteomes:UP000001870};
RX PubMed=18670397; DOI=10.1038/ismej.2008.74;
RA Ivars-Martinez E., Martin-Cuadrado A.B., D'Auria G., Mira A., Ferriera S.,
RA Johnson J., Friedman R., Rodriguez-Valera F.;
RT "Comparative genomics of two ecotypes of the marine planktonic copiotroph
RT Alteromonas macleodii suggests alternative lifestyles associated with
RT different kinds of particulate organic matter.";
RL ISME J. 2:1194-1212(2008).
CC -!- FUNCTION: ATPase that binds to both the 70S ribosome and the 50S
CC ribosomal subunit in a nucleotide-independent manner.
CC {ECO:0000256|HAMAP-Rule:MF_00944}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. OBG GTPase family. YchF/OLA1 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00944}.
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DR EMBL; CP001103; AEA97651.1; -; Genomic_DNA.
DR RefSeq; WP_012517991.1; NC_011138.3.
DR AlphaFoldDB; F2G7K1; -.
DR GeneID; 56341938; -.
DR KEGG; amc:MADE_1007555; -.
DR HOGENOM; CLU_018395_0_1_6; -.
DR OMA; VLRCFDN; -.
DR Proteomes; UP000001870; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0043023; F:ribosomal large subunit binding; IEA:UniProtKB-UniRule.
DR CDD; cd04867; TGS_YchF_OLA1; 1.
DR CDD; cd01900; YchF; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.150.300; TGS-like domain; 1.
DR HAMAP; MF_00944; YchF_OLA1_ATPase; 1.
DR InterPro; IPR004396; ATPase_YchF/OLA1.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR031167; G_OBG.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR023192; TGS-like_dom_sf.
DR InterPro; IPR013029; YchF_C.
DR InterPro; IPR041706; YchF_N.
DR NCBIfam; TIGR00092; redox-regulated ATPase YchF; 1.
DR PANTHER; PTHR23305; OBG GTPASE FAMILY; 1.
DR PANTHER; PTHR23305:SF18; OBG-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF06071; YchF-GTPase_C; 1.
DR PIRSF; PIRSF006641; CHP00092; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR PROSITE; PS51710; G_OBG; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00944}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00944}.
FT DOMAIN 3..256
FT /note="OBG-type G"
FT /evidence="ECO:0000259|PROSITE:PS51710"
FT DOMAIN 278..361
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT BINDING 12..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00944"
SQ SEQUENCE 363 AA; 40026 MW; 4AD5F7FD716F9FCF CRC64;
MGFKCGIVGL PNVGKSTLFN ALTKAGIEAA NFPFCTIEPN TGVVPVPDLR LDKLAEIVNP
QRVIPTTMEF VDIAGLVEGA SKGEGLGNKF LANIRETDAI GHVVRCFDDE NIVHVAGRVS
PKDDIDVINT ELALSDLETT EKALHRVAKR AKGGDADAKY EMKVLEKIKP HLDEGLLLRS
LELSKEELEA ISYMNMLTLK PTMYIANVNE DGFENNPYLD QVKEIAAGEN ATVVAVCASI
ESDIAELEDD EREEFMQDMG LEEPGLNRVI RSGYNLLTLQ TYFTAGVKEV RAWTFPEGST
APQAAGKIHT DFEKGFIRAE IVSYDHFVEF NGEQGAKDAG KWRLEGKDYI VKDGDVIHFR
FNV
//