ID A0A062X3G6_9LACO Unreviewed; 443 AA.
AC A0A062X3G6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, 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=Lani381_1481 {ECO:0000313|EMBL:KDA45303.1};
OS Ligilactobacillus animalis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1605 {ECO:0000313|EMBL:KDA45303.1, ECO:0000313|Proteomes:UP000027129};
RN [1] {ECO:0000313|EMBL:KDA45303.1, ECO:0000313|Proteomes:UP000027129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=381-IL-28 {ECO:0000313|EMBL:KDA45303.1,
RC ECO:0000313|Proteomes:UP000027129};
RA Sturino J.M., Rajendran M., Altermann E.;
RT "Draft Genome Sequence of Lactobacillus animalis 381-IL-28.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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:KDA45303.1}.
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DR EMBL; JMHU01000021; KDA45303.1; -; Genomic_DNA.
DR RefSeq; WP_035448851.1; NZ_POVP01000004.1.
DR AlphaFoldDB; A0A062X3G6; -.
DR GeneID; 61226160; -.
DR PATRIC; fig|1605.9.peg.1452; -.
DR eggNOG; COG0513; Bacteria.
DR OrthoDB; 9805696at2; -.
DR Proteomes; UP000027129; 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:0016874; F:ligase activity; IEA:UniProtKB-KW.
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 Ligase {ECO:0000313|EMBL:KDA45303.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01494}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_01494};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_01494}.
FT DOMAIN 3..31
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 34..207
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 230..385
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 379..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 3..31
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 379..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..443
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 443 AA; 50456 MW; 35E40042E4E72091 CRC64;
MNKTFKDFNL KPFLNEALTE IGFQAPTEVQ KRLIPVIKKG KSVVGQSQTG SGKTHTFLLP
IFNAIDPAVH AVQAVITTPS RELAYQIYGA AKQLAKHSET EILVQNYVGG TDKLRQIEKL
KHHQPQIVIG TPGRILDLMR SNALDVHNAH YLVVDEADMT LDLGFLKETD AIASALPKDL
QMLVFSATIP QKLKPFLQKY MNDPVVEVVE NKTVISPTID NWLLSTKGRD KKQLIYQLLT
MGEPYLALVF ANTKERADEL TTYLRHQGLK VAKIHGGIQP RERKRLMREI QNLEYQYVVA
TDLAARGIDI EGVSHVINDD LPEDLEFFVH RVGRTGRNNL KGIAITLYVP SEEAQIEELE
KMGVTFVPKA LKNGEIVDSY DRNRRQKRRT RQESLDPKMI GMVKKAKKKR KPGYKNKIKR
ALKRDAQQKR KIARRQERKN QRS
//
