YCHF_BACSU
ID YCHF_BACSU Reviewed; 366 AA.
AC P37518;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Ribosome-binding ATPase YchF {ECO:0000255|HAMAP-Rule:MF_00944};
GN Name=ychF {ECO:0000255|HAMAP-Rule:MF_00944}; Synonyms=engD, yyaF;
GN OrderedLocusNames=BSU40920;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=CRK6000;
RX PubMed=12427945; DOI=10.1099/00221287-148-11-3539;
RA Morimoto T., Loh P.C., Hirai T., Asai K., Kobayashi K., Moriya S.,
RA Ogasawara N.;
RT "Six GTP-binding proteins of the Era/Obg family are essential for cell
RT growth in Bacillus subtilis.";
RL Microbiology 148:3539-3552(2002).
RN [4]
RP INDUCTION.
RC STRAIN=168;
RX PubMed=14762004; DOI=10.1128/jb.186.4.1097-1105.2004;
RA Lindner C., Nijland R., van Hartskamp M., Bron S., Hamoen L.W.,
RA Kuipers O.P.;
RT "Differential expression of two paralogous genes of Bacillus subtilis
RT encoding single-stranded DNA binding protein.";
RL J. Bacteriol. 186:1097-1105(2004).
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 -!- INDUCTION: Weakly expressed during exponential growth in rich medium,
CC stops at onset of stationary phase. In minimal medium is more strongly
CC expressed and continues into stationary phase, part of the ychF-rpsF-
CC ssbA-rpsR operon (PubMed:14762004). {ECO:0000269|PubMed:14762004}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:12427945}.
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; D26185; BAA05222.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16129.1; -; Genomic_DNA.
DR PIR; S66016; S66016.
DR RefSeq; NP_391972.1; NC_000964.3.
DR RefSeq; WP_003242727.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P37518; -.
DR SMR; P37518; -.
DR IntAct; P37518; 1.
DR MINT; P37518; -.
DR STRING; 224308.BSU40920; -.
DR jPOST; P37518; -.
DR PaxDb; P37518; -.
DR PRIDE; P37518; -.
DR EnsemblBacteria; CAB16129; CAB16129; BSU_40920.
DR GeneID; 937916; -.
DR KEGG; bsu:BSU40920; -.
DR PATRIC; fig|224308.179.peg.4433; -.
DR eggNOG; COG0012; Bacteria.
DR InParanoid; P37518; -.
DR OMA; VLRCFDN; -.
DR PhylomeDB; P37518; -.
DR BioCyc; BSUB:BSU40920-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
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; cd04867; TGS_YchF_OLA1; 1.
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 2: Evidence at transcript level;
KW ATP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..366
FT /note="Ribosome-binding ATPase YchF"
FT /id="PRO_0000201671"
FT DOMAIN 3..259
FT /note="OBG-type G"
FT DOMAIN 281..364
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT BINDING 12..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00944"
FT BINDING 16
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 366 AA; 40069 MW; D4904E33E79D44C0 CRC64;
MALTAGIVGL PNVGKSTLFN AITQAGAESA NYPFCTIDPN VGIVEVPDDR LQKLTELVNP
KKTVPTAFEF TDIAGIVKGA SKGEGLGNKF LSHIRQVDAI CHVVRAFSDD NITHVSGKVD
PIDDIETINL ELILADMETV EKRITRVSKL AKQKDKDAVF EFEILSKLKE AFESEKPARS
VEFTEEQQKL VKQLHLLTSK PILYVANVSE DEVADPSGNE NVAKIREYAA GENAEVIVVC
AKIESEIAEL EGEEKQMFLE ELGIQESGLD QLIKASYSLL GLATYFTAGE QEVRAWTFKK
GMKAPECAGI IHSDFERGFI RAETVAYEDL LAGGGMAGAK EAGKVRLEGK EYVVQDGDVI
HFRFNV
