ID M5J6N4_9LACO Unreviewed; 442 AA.
AC M5J6N4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
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=D271_01652 {ECO:0000313|EMBL:EKW99535.1};
OS Ligilactobacillus saerimneri 30a.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1227363 {ECO:0000313|EMBL:EKW99535.1, ECO:0000313|Proteomes:UP000011912};
RN [1] {ECO:0000313|EMBL:EKW99535.1, ECO:0000313|Proteomes:UP000011912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=30a {ECO:0000313|EMBL:EKW99535.1,
RC ECO:0000313|Proteomes:UP000011912};
RX PubMed=23405290;
RA Romano A., Trip H., Campbell-Sills H., Bouchez O., Sherman D.,
RA Lolkema J.S., Lucas P.M.;
RT "Genome Sequence of Lactobacillus saerimneri 30a (Formerly Lactobacillus
RT sp. Strain 30a), a Reference Lactic Acid Bacterium Strain Producing
RT Biogenic Amines.";
RL Genome Announc. 1:E00097-E00012(2013).
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:EKW99535.1}.
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DR EMBL; ANAG01000005; EKW99535.1; -; Genomic_DNA.
DR RefSeq; WP_009551799.1; NZ_ANAG01000005.1.
DR AlphaFoldDB; M5J6N4; -.
DR STRING; 1227363.D271_01652; -.
DR GeneID; 80986232; -.
DR PATRIC; fig|1227363.6.peg.321; -.
DR Proteomes; UP000011912; 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:UP000011912};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01494};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_01494}.
FT DOMAIN 1..29
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 32..204
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 231..385
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 399..442
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 428..442
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 50738 MW; 1E992B47F0803F8F CRC64;
MKFTDFEFKP FINDALAEIG FTEPTEVQER LIPMILDGRS VVGQSQTGSG KTHAFLLPIM
QNVTADDYVQ AVITTPSREL AYQIYKAAKQ IVQHADQTIQ VVNYVGGTDK HRQVEKLQHH
QPQIVIGTPG RILDLIRTNA LDIHKAHYFV VDEADMTLDM GFLAPVDAIA STMPQDLQML
VFSATIPVKL QPFLRKYMNN PVVEVVETKT VISPTIENIL ISTQGKDRNR LIYQLLTMGE
PFLALVFANT IKRVDELTAY LRAQGLKVAK IHGDIQPRQR KRIMREVQQL DYQFVVATDL
AARGIDIEGV SLVINDDIPE DLEFFIHRVG RTGRNGMAGT AITLYGPGED QMIVELEKMG
IHFKPQMLRN HELVDSYDRN RRDKRRVRQQ KLDPRLVGMV KKEKKKRKPG YKRKIKQAIQ
KDRQQKKKLE KRQVRRQQRR RG
//
