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Database: UniProt
Entry: P21507
LinkDB: P21507
Original site: P21507 
ID   SRMB_ECOLI              Reviewed;         444 AA.
AC   P21507; Q2MAF4;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   13-NOV-2019, entry version 167.
DE   RecName: Full=ATP-dependent RNA helicase SrmB {ECO:0000255|HAMAP-Rule:MF_00967};
DE            EC=3.6.4.13 {ECO:0000255|HAMAP-Rule:MF_00967};
GN   Name=srmB {ECO:0000255|HAMAP-Rule:MF_00967}; Synonyms=rbaB, rhlA;
GN   OrderedLocusNames=b2576, JW2560;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2461520; DOI=10.1038/336496a0;
RA   Nishi K., Morel-Deville F., Hershey J.W.B., Leighton T., Schnier J.;
RT   "An eIF-4A-like protein is a suppressor of an Escherichia coli mutant
RT   defective in 50S ribosomal subunit assembly.";
RL   Nature 336:496-498(1988).
RN   [2]
RP   ERRATUM, AND SEQUENCE REVISION.
RA   Nishi K., Morel-Deville F., Hershey J.W.B., Leighton T., Schnier J.;
RL   Nature 340:246-246(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RA   Nashimoto H.;
RT   "Non-ribosomal proteins affecting the assembly of ribosomes in
RT   Escherichia coli.";
RL   (In) Nierhaus K.H. (eds.);
RL   The translational apparatus, pp.185-195, Plenum Press, New York
RL   (1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RA   Nashimoto H., Saito N.;
RL   Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [7]
RP   FUNCTION IN 50S RIBOSOME BIOGENESIS, AND DISRUPTION PHENOTYPE.
RC   STRAIN=B / BL21-DE3, and K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=12787353; DOI=10.1046/j.1365-2958.2003.03513.x;
RA   Charollais J., Pflieger D., Vinh J., Dreyfus M., Iost I.;
RT   "The DEAD-box RNA helicase SrmB is involved in the assembly of 50S
RT   ribosomal subunits in Escherichia coli.";
RL   Mol. Microbiol. 48:1253-1265(2003).
RN   [8]
RP   FUNCTION AS RNA-HELICASE, FUNCTION AS ATPASE, AND CATALYTIC ACTIVITY.
RX   PubMed=15196029; DOI=10.1021/bi049852s;
RA   Bizebard T., Ferlenghi I., Iost I., Dreyfus M.;
RT   "Studies on three E. coli DEAD-box helicases point to an unwinding
RT   mechanism different from that of model DNA helicases.";
RL   Biochemistry 43:7857-7866(2004).
RN   [9]
RP   FUNCTION IN 50S RIBOSOME BIOGENESIS, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=15148362; DOI=10.1093/nar/gkh603;
RA   Charollais J., Dreyfus M., Iost I.;
RT   "CsdA, a cold-shock RNA helicase from Escherichia coli, is involved in
RT   the biogenesis of 50S ribosomal subunit.";
RL   Nucleic Acids Res. 32:2751-2759(2004).
RN   [10]
RP   INTERACTION WITH L4, L24 AND 23S RRNA, AND DOMAIN.
RC   STRAIN=B / BL21-DE3;
RX   PubMed=19734346; DOI=10.1093/nar/gkp685;
RA   Trubetskoy D., Proux F., Allemand F., Dreyfus M., Iost I.;
RT   "SrmB, a DEAD-box helicase involved in Escherichia coli ribosome
RT   assembly, is specifically targeted to 23S rRNA in vivo.";
RL   Nucleic Acids Res. 37:6540-6549(2009).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 219-388.
RA   Pietras Z., Hardwick S.W., Luisi B.F.;
RT   "Interactions of Escherichia Coli DEAD-box helicases with the RraA
RT   protein.";
RL   Submitted (MAY-2011) to the PDB data bank.
CC   -!- FUNCTION: DEAD-box RNA helicase involved in the assembly of the
CC       50S ribosomal subunit at low temperature. Exhibits RNA-stimulated
CC       ATP hydrolysis and RNA unwinding activity. Acts before DeaD.
CC       {ECO:0000255|HAMAP-Rule:MF_00967, ECO:0000269|PubMed:12787353,
CC       ECO:0000269|PubMed:15148362, ECO:0000269|PubMed:15196029}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00967,
CC         ECO:0000269|PubMed:15196029};
CC   -!- SUBUNIT: Interacts with the 50S ribosomal subunit. Forms a complex
CC       with the 50S ribosomal proteins L4 and L24, and a region near the
CC       5'-end of 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_00967,
CC       ECO:0000269|PubMed:19734346}.
CC   -!- INTERACTION:
CC       P05055:pnp; NbExp=3; IntAct=EBI-546628, EBI-548080;
CC       P36979:rlmN; NbExp=4; IntAct=EBI-546628, EBI-559071;
CC       P37765:rluB; NbExp=6; IntAct=EBI-546628, EBI-561550;
CC       P21513:rne; NbExp=3; IntAct=EBI-546628, EBI-549958;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00967}.
CC   -!- DOMAIN: The C-terminal extension is not essential for ribosome
CC       assembly, but is important for the formation or the stability of
CC       the complex. {ECO:0000269|PubMed:19734346}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene grow very poorly at
CC       20 degrees Celsius, show a severe deficit of free 50S ribosomal
CC       subunits and accumulate an abnormal large ribosomal subunit.
CC       Disruption also impairs the processing of both 23S and 16S rRNAs.
CC       {ECO:0000269|PubMed:12787353, ECO:0000269|PubMed:15148362}.
CC   -!- MISCELLANEOUS: Overexpression suppresses a mutant defective in 50S
CC       ribosomal subunit assembly. {ECO:0000305|PubMed:2461520}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. SrmB
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00967}.
DR   EMBL; X14152; CAA32364.1; -; Genomic_DNA.
DR   EMBL; D13169; BAA02447.1; -; Genomic_DNA.
DR   EMBL; D64044; BAA10922.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75629.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76752.1; -; Genomic_DNA.
DR   PIR; G65035; G65035.
DR   RefSeq; NP_417071.1; NC_000913.3.
DR   RefSeq; WP_000219203.1; NZ_LN832404.1.
DR   PDB; 2YJT; X-ray; 2.90 A; D=219-388.
DR   PDBsum; 2YJT; -.
DR   SMR; P21507; -.
DR   BioGrid; 4263366; 231.
DR   BioGrid; 851393; 5.
DR   DIP; DIP-10920N; -.
DR   IntAct; P21507; 34.
DR   STRING; 511145.b2576; -.
DR   EPD; P21507; -.
DR   jPOST; P21507; -.
DR   PaxDb; P21507; -.
DR   PRIDE; P21507; -.
DR   EnsemblBacteria; AAC75629; AAC75629; b2576.
DR   EnsemblBacteria; BAE76752; BAE76752; BAE76752.
DR   GeneID; 947055; -.
DR   KEGG; ecj:JW2560; -.
DR   KEGG; eco:b2576; -.
DR   PATRIC; fig|1411691.4.peg.4158; -.
DR   EchoBASE; EB0968; -.
DR   eggNOG; ENOG4105C1J; Bacteria.
DR   eggNOG; COG0513; LUCA.
DR   HOGENOM; HOG000268807; -.
DR   InParanoid; P21507; -.
DR   KO; K05590; -.
DR   PhylomeDB; P21507; -.
DR   BioCyc; EcoCyc:EG10975-MONOMER; -.
DR   BioCyc; ECOL316407:JW2560-MONOMER; -.
DR   PRO; PR:P21507; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
DR   GO; GO:0008143; F:poly(A) binding; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IDA:UniProtKB.
DR   GO; GO:0033592; F:RNA strand annealing activity; IDA:EcoCyc.
DR   GO; GO:0008186; F:RNA-dependent ATPase activity; IDA:UniProtKB.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; IMP:EcoCyc.
DR   HAMAP; MF_00967; DEAD_helicase_SrmB; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR028621; DEAD_helicase_SrmB.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
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; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Complete proteome; Cytoplasm; Helicase;
KW   Hydrolase; Nucleotide-binding; Reference proteome;
KW   Ribosome biogenesis; RNA-binding.
FT   CHAIN         1    444       ATP-dependent RNA helicase SrmB.
FT                                /FTId=PRO_0000055109.
FT   DOMAIN       35    209       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00967}.
FT   DOMAIN      238    387       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00967}.
FT   NP_BIND      48     55       ATP. {ECO:0000255|HAMAP-Rule:MF_00967}.
FT   MOTIF         4     32       Q motif.
FT   MOTIF       157    160       DEAD box.
FT   STRAND      223    231       {ECO:0000244|PDB:2YJT}.
FT   HELIX       232    243       {ECO:0000244|PDB:2YJT}.
FT   STRAND      250    254       {ECO:0000244|PDB:2YJT}.
FT   STRAND      256    258       {ECO:0000244|PDB:2YJT}.
FT   HELIX       259    272       {ECO:0000244|PDB:2YJT}.
FT   STRAND      276    278       {ECO:0000244|PDB:2YJT}.
FT   HELIX       284    294       {ECO:0000244|PDB:2YJT}.
FT   STRAND      301    304       {ECO:0000244|PDB:2YJT}.
FT   HELIX       307    309       {ECO:0000244|PDB:2YJT}.
FT   STRAND      319    324       {ECO:0000244|PDB:2YJT}.
FT   HELIX       329    335       {ECO:0000244|PDB:2YJT}.
FT   HELIX       336    338       {ECO:0000244|PDB:2YJT}.
FT   STRAND      342    344       {ECO:0000244|PDB:2YJT}.
FT   STRAND      347    353       {ECO:0000244|PDB:2YJT}.
FT   HELIX       354    356       {ECO:0000244|PDB:2YJT}.
FT   HELIX       357    366       {ECO:0000244|PDB:2YJT}.
FT   STRAND      367    369       {ECO:0000244|PDB:2YJT}.
FT   STRAND      377    379       {ECO:0000244|PDB:2YJT}.
SQ   SEQUENCE   444 AA;  49914 MW;  1A459538A25807A7 CRC64;
     MTVTTFSELE LDESLLEALQ DKGFTRPTAI QAAAIPPALD GRDVLGSAPT GTGKTAAYLL
     PALQHLLDFP RKKSGPPRIL ILTPTRELAM QVSDHARELA KHTHLDIATI TGGVAYMNHA
     EVFSENQDIV VATTGRLLQY IKEENFDCRA VETLILDEAD RMLDMGFAQD IEHIAGETRW
     RKQTLLFSAT LEGDAIQDFA ERLLEDPVEV SANPSTRERK KIHQWYYRAD DLEHKTALLV
     HLLKQPEATR SIVFVRKRER VHELANWLRE AGINNCYLEG EMVQGKRNEA IKRLTEGRVN
     VLVATDVAAR GIDIPDVSHV FNFDMPRSGD TYLHRIGRTA RAGRKGTAIS LVEAHDHLLL
     GKVGRYIEEP IKARVIDELR PKTRAPSEKQ TGKPSKKVLA KRAEKKKAKE KEKPRVKKRH
     RDTKNIGKRR KPSGTGVPPQ TTEE
//
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