YCHF_MYCPN
ID YCHF_MYCPN Reviewed; 362 AA.
AC P75088;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Ribosome-binding ATPase YchF {ECO:0000255|HAMAP-Rule:MF_00944};
GN Name=ychF {ECO:0000255|HAMAP-Rule:MF_00944}; OrderedLocusNames=MPN_026;
GN ORFNames=B01_orf362, MP128;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
CC -!- FUNCTION: ATPase that binds to both the 70S ribosome and the 50S
CC ribosomal subunit in a nucleotide-independent manner.
CC {ECO:0000255|HAMAP-Rule:MF_00944}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. OBG GTPase family. YchF/OLA1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00944}.
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DR EMBL; U00089; AAB95776.1; -; Genomic_DNA.
DR PIR; S73454; S73454.
DR RefSeq; NP_109714.1; NC_000912.1.
DR AlphaFoldDB; P75088; -.
DR SMR; P75088; -.
DR STRING; 272634.MPN_026; -.
DR EnsemblBacteria; AAB95776; AAB95776; MPN_026.
DR KEGG; mpn:MPN_026; -.
DR PATRIC; fig|272634.6.peg.25; -.
DR HOGENOM; CLU_018395_0_1_14; -.
DR OMA; VLRCFDN; -.
DR BioCyc; MPNE272634:G1GJ3-39-MON; -.
DR Proteomes; UP000000808; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043023; F:ribosomal large subunit binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule.
DR CDD; cd01900; YchF; 1.
DR Gene3D; 1.10.150.300; -; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF06071; YchF-GTPase_C; 1.
DR PIRSF; PIRSF006641; CHP00092; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR TIGRFAMs; TIGR00092; TIGR00092; 1.
DR PROSITE; PS51710; G_OBG; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW ATP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..362
FT /note="Ribosome-binding ATPase YchF"
FT /id="PRO_0000122459"
FT DOMAIN 2..258
FT /note="OBG-type G"
FT DOMAIN 281..347
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT BINDING 11..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00944"
FT BINDING 15
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 35
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 362 AA; 40607 MW; 7C79B46C84D5FF83 CRC64;
MLSAGIVGLP NVGKSTLFSA ITNLQVEIAN YPFATIEPNA GIVNVIDERL DKLASLIKPD
KVTHTTFRFV DIAGLVKGAS KGEGLGNQFL ANIREVDLIC HVVRCYEDKK IVHVNNQVDP
VFDFEIIVNE LIQADIEVVN TRIGKIKRKA ESGDKQSKEE YQLLAPVLQG LQQNQMVLHL
VNEVDLKKLK SLNLLTAKPI LVVANVSEAD LSNLDHNPHL TQLNQFLKQH NLPHAIPVCA
LLENELSSLD ANGRQDWLKE LGLSDYQGLN QLIKTAYDAI GLWSFFTFGK QEVRAWAFKK
GWLAPQCAGE IHTDFERGFI KVEVISWNQL YELKSLQEAK KQGLVRLRGQ GLRDARWWCV
SL