ID   CSHA_STRR6              Reviewed;         524 AA.
AC   P0A4D8; P35599;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=DEAD-box ATP-dependent RNA helicase CshA {ECO:0000255|HAMAP-Rule:MF_01493};
DE            EC=3.6.4.13 {ECO:0000255|HAMAP-Rule:MF_01493};
DE   AltName: Full=Exported protein 9;
GN   Name=cshA {ECO:0000255|HAMAP-Rule:MF_01493}; Synonyms=exp9;
GN   OrderedLocusNames=spr1440;
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-255 / R6;
RX   PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA   Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA   DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA   Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA   McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA   Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA   Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA   Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 107-219, AND SUBCELLULAR LOCATION.
RX   PubMed=7934910; DOI=10.1111/j.1365-2958.1993.tb01233.x;
RA   Pearce B.J., Yin Y.B., Masure H.R.;
RT   "Genetic identification of exported proteins in Streptococcus pneumoniae.";
RL   Mol. Microbiol. 9:1037-1050(1993).
CC   -!- FUNCTION: DEAD-box RNA helicase possibly involved in RNA degradation.
CC       Unwinds dsRNA in both 5'- and 3'-directions, has RNA-dependent ATPase
CC       activity. {ECO:0000255|HAMAP-Rule:MF_01493}.
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_01493};
CC   -!- SUBUNIT: Oligomerizes, may be a member of the RNA degradosome.
CC       {ECO:0000255|HAMAP-Rule:MF_01493}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01493}. Cell
CC       membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. CshA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01493}.
CC   -!- CAUTION: Has been suggested to be found on the cell surface, but its
CC       function as an RNA helicase makes this dubious.
CC       {ECO:0000305|PubMed:7934910}.
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DR   EMBL; AE007317; AAL00244.1; -; Genomic_DNA.
DR   EMBL; L20563; AAA26885.1; -; Genomic_DNA.
DR   PIR; G98051; G98051.
DR   RefSeq; NP_359033.1; NC_003098.1.
DR   RefSeq; WP_000671113.1; NC_003098.1.
DR   AlphaFoldDB; P0A4D8; -.
DR   SMR; P0A4D8; -.
DR   STRING; 171101.spr1440; -.
DR   EnsemblBacteria; AAL00244; AAL00244; spr1440.
DR   GeneID; 60234437; -.
DR   KEGG; spr:spr1440; -.
DR   PATRIC; fig|171101.6.peg.1556; -.
DR   eggNOG; COG0513; Bacteria.
DR   HOGENOM; CLU_003041_21_0_9; -.
DR   OMA; EHKDGQR; -.
DR   Proteomes; UP000000586; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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   GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0010501; P:RNA secondary structure unwinding; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_01493; DEAD_helicase_CshA; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR030880; DEAD_helicase_CshA.
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   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Cytoplasm; Helicase; Hydrolase; Membrane;
KW   Nucleotide-binding; Reference proteome; RNA-binding; Stress response.
FT   CHAIN           1..524
FT                   /note="DEAD-box ATP-dependent RNA helicase CshA"
FT                   /id="PRO_0000055120"
FT   DOMAIN          32..202
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
FT   DOMAIN          213..373
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
FT   REGION          440..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1..29
FT                   /note="Q motif"
FT   MOTIF           150..153
FT                   /note="DEAD box"
FT   COMPBIAS        459..508
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         45..52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
FT   CONFLICT        203
FT                   /note="K -> R (in Ref. 2; AAA26885)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   524 AA;  58827 MW;  B6523D038C2F1EF4 CRC64;
     MKFNELNLSA DLLAEIEKAG FVEASPIQEQ TIPLALEGKD VIGQAQTGTG KTAAFGLPTL
     EKIRTEEATI QALVIAPTRE LAVQSQEELF RFGRSKGVKV RSVYGGSSIE KQIKALKSGA
     HIVVGTPGRL LDLIKRKALK LQDIETLILD EADEMLNMGF LEDIEAIISR VPENRQTLLF
     SATMPDAIKR IGVQFMKAPE HVKIAAKELT TELVDQYYIR VKEQEKFDTM TRLMDVAQPE
     LAIVFGRTKR RVDELTRGLK IRGFRAEGIH GDLDQNKRLR VLRDFKNGNL DVLVATDVAA
     RGLDISGVTH VYNYDIPQDP ESYVHRIGRT GRAGKSGQSI TFVAPNEMGY LQIIENLTKK
     RMKGLKPASV EESFQSKKQV ALKKIERDFA DETIRANFEK FGKDARKLAA EFTPEELAMY
     ILSLTVQDPD SLPEVEIARE KPLPFKPSGN GFGGKAKGGR GGRRGDDRRE RDRRGNGRRD
     EFKKGSRGND RFDKEKRYRK DNKKPRNTLS EKQTGFVIRN KGDK