ID   CSHA_LIMRT              Reviewed;         497 AA.
AC   Q9Z6C9;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=ATP-dependent RNA helicase CshA;
DE            EC=3.6.4.13 {ECO:0000255|HAMAP-Rule:MF_01493};
DE   AltName: Full=Autoaggregation-mediating protein;
GN   Name=cshA {ECO:0000255|HAMAP-Rule:MF_01493}; Synonyms=aggH;
OS   Limosilactobacillus reuteri (Lactobacillus reuteri).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=1598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 53608 / 1063;
RX   PubMed=10231497; DOI=10.1046/j.1365-2958.1999.01363.x;
RA   Roos S., Lindgren S., Jonsson H.;
RT   "Autoaggregation of Lactobacillus reuteri is mediated by a putative DEAD-
RT   box helicase.";
RL   Mol. Microbiol. 32:427-436(1999).
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 (By similarity). Over-expression leads to cell aggregation.
CC       {ECO:0000255|HAMAP-Rule:MF_01493, ECO:0000269|PubMed:10231497}.
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       Extracellular side {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Loss of cellular aggregation.
CC       {ECO:0000269|PubMed:10231497}.
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:10231497}.
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DR   EMBL; AF091502; AAD20136.1; -; Genomic_DNA.
DR   RefSeq; WP_003674631.1; NZ_RIAU01000001.1.
DR   AlphaFoldDB; Q9Z6C9; -.
DR   SMR; Q9Z6C9; -.
DR   PRIDE; Q9Z6C9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-UniRule.
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; RNA-binding; Stress response.
FT   CHAIN           1..497
FT                   /note="ATP-dependent RNA helicase CshA"
FT                   /id="PRO_0000430101"
FT   DOMAIN          32..202
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
FT   DOMAIN          228..373
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
FT   REGION          425..497
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        457..476
FT                   /note="Basic 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"
SQ   SEQUENCE   497 AA;  56481 MW;  28196704FB77553C CRC64;
     MKFSELGLSD SLLKAIKRSG YEEATPIQEQ TIPMVLEGKD VIGQAQTGTG KTAAFGLPII
     ENVDTENPNI QAIIISPTRE LAIQTQEELY RLGKDKHVRV QVVYGGADIR RQIKSLKQHP
     QILVGTPGRL RDHINRHTVK LDHIKTLVLD EADEMLNMGF LEDIESIIKE TPDDRQTLLF
     SATMPPEIKR IGVQFMSDPE TVRIKAKELT TDLVDQYYVR ARDYEKFDIM TRLIDVQDPD
     LTIVFGRTKR RVDELSKGLI ARGYNAAGIH GDLTQDKRSK IMWKFKNNEL DILVATDVAA
     RGLDISGVTH VYNYDIPSDP DSYVHRIGRT GRAGHHGVSL TFVTPNEMDY LHEIEKLTRV
     RMLPLKPPTA EEAFKGQVAS AFNDIDELIA QDSTDRYEEA AEKLLETHNA TDLVAALLNN
     MTKEAASEVP VKITPERPLP RRNKRNNRNG NRNNSHGGNH YRRKNFRRHQ HGSHRNDNHG
     KSHSSRHSFN IRHRKEN