ID A0A2A4E985_9MICO Unreviewed; 357 AA.
AC A0A2A4E985;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Ribosome-binding ATPase YchF {ECO:0000256|HAMAP-Rule:MF_00944};
GN Name=ychF {ECO:0000256|HAMAP-Rule:MF_00944};
GN ORFNames=AUC47_03560 {ECO:0000313|EMBL:PCE14321.1};
OS Microbacterium sp. SZ1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1849736 {ECO:0000313|EMBL:PCE14321.1, ECO:0000313|Proteomes:UP000217958};
RN [1] {ECO:0000313|EMBL:PCE14321.1, ECO:0000313|Proteomes:UP000217958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZ1 {ECO:0000313|EMBL:PCE14321.1,
RC ECO:0000313|Proteomes:UP000217958};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:PCE14321.1}.
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DR EMBL; LPVV01000034; PCE14321.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A4E985; -.
DR OrthoDB; 9810373at2; -.
DR Proteomes; UP000217958; Unassembled WGS sequence.
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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00944}.
FT DOMAIN 3..250
FT /note="OBG-type G"
FT /evidence="ECO:0000259|PROSITE:PS51710"
FT DOMAIN 272..355
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT COILED 130..157
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 12..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00944"
SQ SEQUENCE 357 AA; 38193 MW; FA9972486FB0A55B CRC64;
MALTIGIVGL PNVGKSTLFN ALTKNDVLAA NYPFATIEPN VGVVNLPDPR LDKLAEIFHS
ERILPAAVSF VDIAGIVRGA SEGEGLGNKF LANIREADAI AQVVRGFADD DVVHVDGAVN
PASDMETINA ELMLADLETV EKAITRYEKE VRGKKIEPVV LETAKAAKDA LERGILLSVS
GLDLAPIREL GLLTSKPVIF VFNVDEGVLT DTARKEELAA LVAPAKAIFL DAKIESELKD
LDPEDAAELL ASTGQDESGL DQLARIGFDT LGLQTYLTAG PKEARAWTIP KGSKAPQAAG
VIHTDFEKGF IKAEIVSFDD LVETGSVVEA RAKGKARLEG KDYVMQDGDV VEFRFNN
//