ID   YFML_BACSU              Reviewed;         376 AA.
AC   O34750; Q79ES5;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Probable ATP-dependent RNA helicase YfmL;
DE            EC=3.6.4.13;
GN   Name=yfmL; OrderedLocusNames=BSU07430;
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 / AC327;
RX   PubMed=9272861; DOI=10.1016/s0378-1119(97)00130-3;
RA   Yamamoto H., Uchiyama S., Nugroho F.A., Sekiguchi J.;
RT   "Cloning and sequencing of a 35.7 kb in the 70 degree-73 degree region of
RT   the Bacillus subtilis genome reveal genes for a new two-component system,
RT   three spore germination proteins, an iron uptake system and a general
RT   stress response protein.";
RL   Gene 194:191-199(1997).
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   DISCUSSION OF POSSIBLE FUNCTION.
RC   STRAIN=168;
RX   PubMed=20572937; DOI=10.1111/j.1365-2958.2010.07264.x;
RA   Lehnik-Habrink M., Pfortner H., Rempeters L., Pietack N., Herzberg C.,
RA   Stulke J.;
RT   "The RNA degradosome in Bacillus subtilis: identification of CshA as the
RT   major RNA helicase in the multiprotein complex.";
RL   Mol. Microbiol. 77:958-971(2010).
RN   [4]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=23175651; DOI=10.1128/jb.01475-12;
RA   Lehnik-Habrink M., Rempeters L., Kovacs A.T., Wrede C., Baierlein C.,
RA   Krebber H., Kuipers O.P., Stulke J.;
RT   "DEAD-box RNA helicases in Bacillus subtilis have multiple functions and
RT   act independently from each other.";
RL   J. Bacteriol. 195:534-544(2013).
CC   -!- FUNCTION: A probable DEAD-box RNA helicase that plays a role in
CC       ribosomal 50S subunit assembly. May be a non-specific RNA helicase.
CC       {ECO:0000269|PubMed:23175651}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- INDUCTION: In rich medium highest expression in exponential growth,
CC       expression decreases in stationary phase (at protein level).
CC       {ECO:0000269|PubMed:23175651}.
CC   -!- DISRUPTION PHENOTYPE: No visible effect at 37 degrees Celsius,
CC       decreased growth at 16 degrees Celsius. A quadruple disruption of all
CC       RNA helicases (cshA, cshB, deaD, yfmL) is not lethal at 37 degrees
CC       Celsius, although both 50S and 70S ribosomes are decreased, while
CC       growth stops at 16 degrees. {ECO:0000269|PubMed:23175651}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. {ECO:0000305}.
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DR   EMBL; D86417; BAA22326.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12572.1; -; Genomic_DNA.
DR   PIR; C69813; C69813.
DR   RefSeq; NP_388624.1; NC_000964.3.
DR   RefSeq; WP_003233750.1; NZ_JNCM01000032.1.
DR   AlphaFoldDB; O34750; -.
DR   SMR; O34750; -.
DR   STRING; 224308.BSU07430; -.
DR   PaxDb; O34750; -.
DR   PRIDE; O34750; -.
DR   EnsemblBacteria; CAB12572; CAB12572; BSU_07430.
DR   GeneID; 938792; -.
DR   KEGG; bsu:BSU07430; -.
DR   PATRIC; fig|224308.179.peg.806; -.
DR   eggNOG; COG0513; Bacteria.
DR   InParanoid; O34750; -.
DR   OMA; TYEDRHT; -.
DR   PhylomeDB; O34750; -.
DR   BioCyc; BSUB:BSU07430-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR   GO; GO:0033592; F:RNA strand annealing activity; IBA:GO_Central.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Reference proteome;
KW   Ribosome biogenesis; RNA-binding.
FT   CHAIN           1..376
FT                   /note="Probable ATP-dependent RNA helicase YfmL"
FT                   /id="PRO_0000360838"
FT   DOMAIN          35..205
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          231..374
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           153..156
FT                   /note="DEAD box"
FT   BINDING         48..55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   376 AA;  42189 MW;  6D5E4B6FAA4723E6 CRC64;
     MTQTWPFLHN AQSFIQENWN ASGFQKPTPV QEQAAQLIMD GKDVIAESPT GTGKTLAYAL
     PVLERIKPEQ KHPQAVILAP SRELVMQIFQ VIQDWKAGSE LRAASLIGGA NVKKQVEKLK
     KHPHIIVGTP GRVFELIKAK KLKMHEVKTI VLDETDQLVL PEHRETMKQI IKTTLRDRQL
     LCFSATLKKE TEDVLRELAQ EPEVLKVQRS KAEAGKVKHQ YLICDQRDKV KLLQKLSRLE
     GMQALVFVRD IGNLSVYAEK LAYHHVELGV LHSEAKKMER AKIIATFEDG EFPLLLATDI
     AARGLDIENL PYVIHADIPD EDGYVHRSGR TGRAGKEGNV LSLVTKLEES KLKKMAKKLG
     VELSEAVYAG GKLKTK