ID G8PB02_PEDCP Unreviewed; 368 AA.
AC G8PB02;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Ribosome-binding ATPase YchF {ECO:0000256|HAMAP-Rule:MF_00944};
GN Name=ychF {ECO:0000256|HAMAP-Rule:MF_00944};
GN OrderedLocusNames=PECL_1653 {ECO:0000313|EMBL:AEV95870.1};
OS Pediococcus claussenii (strain ATCC BAA-344 / DSM 14800 / JCM 18046 / KCTC
OS 3811 / P06).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus.
OX NCBI_TaxID=701521 {ECO:0000313|EMBL:AEV95870.1, ECO:0000313|Proteomes:UP000005444};
RN [1] {ECO:0000313|Proteomes:UP000005444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-344 / DSM 14800 / JCM 18046 / KCTC 3811 / P06
RC {ECO:0000313|Proteomes:UP000005444};
RA Pittet V., Abegunde T., Marfleet T., Haakensen M., Morrow K.,
RA Jayaprakash T., Schroeder K., Trost B., Byrns S., Bergsveinson J.,
RA Kusalik A., Ziola B.;
RT "Genome and plasmid sequences for the beer-spoilage organism Pediococcus
RT claussenii ATCC BAA-344T.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEV95870.1, ECO:0000313|Proteomes:UP000005444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-344 / DSM 14800 / JCM 18046 / KCTC 3811 / P06
RC {ECO:0000313|Proteomes:UP000005444};
RX PubMed=22328764; DOI=10.1128/JB.06759-11;
RA Pittet V., Abegunde T., Marfleet T., Haakensen M., Morrow K.,
RA Jayaprakash T., Schroeder K., Trost B., Byrns S., Bergsveinson J.,
RA Kusalik A., Ziola B.;
RT "Complete Genome Sequence of the Beer Spoilage Organism Pediococcus
RT claussenii ATCC BAA-344T.";
RL J. Bacteriol. 194:1271-1272(2012).
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}.
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; CP003137; AEV95870.1; -; Genomic_DNA.
DR RefSeq; WP_014216064.1; NC_016605.1.
DR AlphaFoldDB; G8PB02; -.
DR STRING; 701521.PECL_1653; -.
DR KEGG; pce:PECL_1653; -.
DR PATRIC; fig|701521.8.peg.1554; -.
DR eggNOG; COG0012; Bacteria.
DR HOGENOM; CLU_018395_0_1_9; -.
DR Proteomes; UP000005444; 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}; Reference proteome {ECO:0000313|Proteomes:UP000005444}.
FT DOMAIN 3..261
FT /note="OBG-type G"
FT /evidence="ECO:0000259|PROSITE:PS51710"
FT DOMAIN 283..366
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 368 AA; 40495 MW; 04D8AB251E750C80 CRC64;
MALTAGIVGL PNVGKSTLFN AITKAGAEMA NYPFATIDPN VGMVEVPDAR LDRIQEIIPA
DKIVHTTFEF TDIAGIVKGA SKGEGLGNKF LENIRQVDAI VHVVRAFDDD NITTVSGKVD
PIEDIQTINM ELSLADLDAI DKRISKVQRA AKGRDKDAVA ELAVLEKIKP VLEEGKAVRT
IEFDEMEQSI VKGLFLLTSK PVLYVANIAE DDMAEPESSK YFNTIKDYVA QEDPEAEVLG
ISAETEQEIA ELEDEDKADF LEAEGIEEPG LNRLIRASYH LLGLQTFFTA GGKETRAWTF
KKGMTAPQTA GVIHSDFERG FIRAETVSFD DLDKYGSMQG VKEAGRLRLE GKDYLVQDGD
IIEFRFNV
//
