ID A0A0R1J9X7_9LACO Unreviewed; 513 AA.
AC A0A0R1J9X7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=DEAD-box ATP-dependent RNA helicase CshA {ECO:0000256|HAMAP-Rule:MF_01493};
DE EC=3.6.4.13 {ECO:0000256|HAMAP-Rule:MF_01493};
GN Name=cshA {ECO:0000256|HAMAP-Rule:MF_01493};
GN ORFNames=FC72_GL001655 {ECO:0000313|EMBL:KRK65028.1};
OS Companilactobacillus tucceti DSM 20183.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Companilactobacillus.
OX NCBI_TaxID=1423811 {ECO:0000313|EMBL:KRK65028.1, ECO:0000313|Proteomes:UP000050929};
RN [1] {ECO:0000313|EMBL:KRK65028.1, ECO:0000313|Proteomes:UP000050929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20183 {ECO:0000313|EMBL:KRK65028.1,
RC ECO:0000313|Proteomes:UP000050929};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:0000256|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:0000256|HAMAP-Rule:MF_01493};
CC -!- SUBUNIT: Oligomerizes, may be a member of the RNA degradosome.
CC {ECO:0000256|HAMAP-Rule:MF_01493}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01493}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. CshA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01493}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRK65028.1}.
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DR EMBL; AZDG01000005; KRK65028.1; -; Genomic_DNA.
DR RefSeq; WP_057764764.1; NZ_AZDG01000005.1.
DR AlphaFoldDB; A0A0R1J9X7; -.
DR STRING; 1423811.FC72_GL001655; -.
DR PATRIC; fig|1423811.3.peg.1690; -.
DR OrthoDB; 9805696at2; -.
DR Proteomes; UP000050929; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; 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 CDD; cd00268; DEADc; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR47963; DEAD-BOX ATP-DEPENDENT RNA HELICASE 47, MITOCHONDRIAL; 1.
DR PANTHER; PTHR47963:SF5; DEAD-BOX ATP-DEPENDENT RNA HELICASE CSHA; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01493}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01493};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01493};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01493};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01493}; Reference proteome {ECO:0000313|Proteomes:UP000050929};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01493};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_01493}.
FT DOMAIN 1..29
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 32..202
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 213..374
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 433..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..29
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 462..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 513 AA; 57438 MW; 7C7AFB29649883C2 CRC64;
MKFNELNLDS KLLSAVDEAG FEETTPIQAQ TIPLVLAGDD VIGQAQTGTG KTAAFGLPIL
DAVDMASNDI QALIISPTRE LAIQTQEELY KLGRKKKVRV QSVYGGSDIR RQIRSLKNHP
NVLVGTPGRL LDHINRHTVK LANVKTVVLD EADEMLDMGF VEDIESILSN VPHEHQTLLF
SATMPKPIMK IADKFMTDPK IVKIKSKELT ADNIDQYFVK SRDFEKFDLM TRIFDVQAPE
LALIFGRTKR RVDELTRGLQ ARGYNAEGIH GDLSQDKRTS VLRKFKAGKL DYLVATDVAA
RGLDISGVSH VYNYDIPQDP DSYVHRIGRT GRAGHSGVSV TFVTPNEMSY LRTIENLTKK
RMTPLAPPSD NEVLKGQMES VKEEIKDTLA NNNLDRFDDI VKELLGEYSP EDLVKVLLND
MIKDAESVPV KIAPERPLPS RKVSRNKSGH GRRYRGNGGN YRGGRNDHRS RRHDDHRGGH
SNHSNSDKRR SNNGGNKKKQ GQSKKSFKIR TTI
//
