ID A0A0R1WUD8_9LACO Unreviewed; 440 AA.
AC A0A0R1WUD8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=DEAD-box ATP-dependent RNA helicase CshB {ECO:0000256|HAMAP-Rule:MF_01494};
DE EC=3.6.4.13 {ECO:0000256|HAMAP-Rule:MF_01494};
GN Name=cshB {ECO:0000256|HAMAP-Rule:MF_01494};
GN ORFNames=FC40_GL000524 {ECO:0000313|EMBL:KRM18742.1};
OS Ligilactobacillus hayakitensis DSM 18933 = JCM 14209.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1423755 {ECO:0000313|EMBL:KRM18742.1, ECO:0000313|Proteomes:UP000051054};
RN [1] {ECO:0000313|EMBL:KRM18742.1, ECO:0000313|Proteomes:UP000051054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18933 {ECO:0000313|EMBL:KRM18742.1,
RC ECO:0000313|Proteomes:UP000051054};
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: Probable DEAD-box RNA helicase. May work in conjunction with
CC the cold shock proteins to ensure proper initiation of transcription at
CC low and optimal temperatures. {ECO:0000256|HAMAP-Rule:MF_01494}.
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_01494};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01494}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. CshB subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01494}.
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:KRM18742.1}.
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DR EMBL; AZGD01000090; KRM18742.1; -; Genomic_DNA.
DR RefSeq; WP_025021886.1; NZ_BAML01000003.1.
DR AlphaFoldDB; A0A0R1WUD8; -.
DR STRING; 1423755.FC40_GL000524; -.
DR PATRIC; fig|1423755.3.peg.577; -.
DR eggNOG; COG0513; Bacteria.
DR OrthoDB; 9805696at2; -.
DR Proteomes; UP000051054; 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:0009409; P:response to cold; IEA:InterPro.
DR GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
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_01494; DEAD_helicase_CshB; 1.
DR InterPro; IPR030881; CshB.
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 InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR47963; DEAD-BOX ATP-DEPENDENT RNA HELICASE 47, MITOCHONDRIAL; 1.
DR PANTHER; PTHR47963:SF1; DEAD-BOX ATP-DEPENDENT RNA HELICASE CSHB; 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; 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_01494}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01494};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01494};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01494};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01494}; Reference proteome {ECO:0000313|Proteomes:UP000051054};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01494};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_01494}.
FT DOMAIN 2..30
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 33..206
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 229..376
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 383..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2..30
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 383..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..417
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 440 AA; 50615 MW; CC1D2ECE6B3737D6 CRC64;
MKKFADYNFV GYINEALKEK NFIEPTKVQE KIIPLVLKGK SVVGQSQTGS GKTHAFLLPI
FQKLDLDNEN LQVIITTPSR ELAYQIYEDA KQIAKFADKK VWMQNCVGGT DKQRQIEKVK
NHQPQLVIGT PGRILDLIKE NALDPRYVKF LVVDEADMTL DLGFLNETDQ IASSLPQDLQ
MLVFSATIPE KLKPFLRKYM ANPEIQVIEN KSIISPTIDN WLISTKGRDK NQLIYNLLTI
GEPYLALIFA NTKERVDQLT QFLRAQGLKV AKIHGGIQPR ERKRVMKGIQ KLDYQFVVAT
DLAARGIDIE GVSHVINDDI PDDLEFFVHR VGRTGRNGMQ GTAITLYEPS EDVLIEELES
MGITFEPKAY KDGEIVDSYD RNRREKRRTK KDAMDPKLRG FVKKQKAKRK PGYKKKIQRR
IKKDEQQKRR IARRQARKMK
//
