ID   RHLB_VIBVU              Reviewed;         435 AA.
AC   Q8DDN6;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=ATP-dependent RNA helicase RhlB {ECO:0000255|HAMAP-Rule:MF_00661};
DE            EC=3.6.4.13 {ECO:0000255|HAMAP-Rule:MF_00661};
GN   Name=rhlB {ECO:0000255|HAMAP-Rule:MF_00661}; OrderedLocusNames=VV1_0939;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DEAD-box RNA helicase involved in RNA degradation. Has RNA-
CC       dependent ATPase activity and unwinds double-stranded RNA.
CC       {ECO:0000255|HAMAP-Rule:MF_00661}.
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_00661};
CC   -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein
CC       complex involved in RNA processing and mRNA degradation.
CC       {ECO:0000255|HAMAP-Rule:MF_00661}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00661}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. RhlB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00661}.
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DR   EMBL; AE016795; AAO09436.1; -; Genomic_DNA.
DR   RefSeq; WP_011078988.1; NC_004459.3.
DR   AlphaFoldDB; Q8DDN6; -.
DR   SMR; Q8DDN6; -.
DR   EnsemblBacteria; AAO09436; AAO09436; VV1_0939.
DR   KEGG; vvu:VV1_0939; -.
DR   HOGENOM; CLU_003041_1_3_6; -.
DR   OMA; EYCTPIQ; -.
DR   Proteomes; UP000002275; Chromosome 1.
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   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_00661; DEAD_helicase_RhlB; 1.
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; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR023554; RNA_helicase_ATP-dep_RhlB.
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; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding;
KW   RNA-binding.
FT   CHAIN           1..435
FT                   /note="ATP-dependent RNA helicase RhlB"
FT                   /id="PRO_0000200788"
FT   DOMAIN          40..219
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00661"
FT   DOMAIN          245..390
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00661"
FT   REGION          395..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           9..37
FT                   /note="Q motif"
FT   MOTIF           165..168
FT                   /note="DEAD box"
FT   COMPBIAS        398..417
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..435
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         53..60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00661"
SQ   SEQUENCE   435 AA;  48744 MW;  E31E7EA0B938001A CRC64;
     MKKTHITEQK FADLGLNPQV VEGLEKKGFE FCTPIQALAL PVLLSGQDIA GQAQTGTGKT
     LAFLTATFNH LLTTPAHEGR QPTQPRAIIM APTRELAIQI YNDAEPLIAS TGIKAALAYG
     GESYDKQLTK LQGGVDVLIG TTGRIIDFYK QRVFNLNNIQ AVVLDEADRM FDLGFIKDIR
     FLFRRMPAPQ ERLNMLFSAT LSYRVQELAF EHMHNPEHVV VEPEQKTGHR IQEELFYPSN
     EDKMALLQTL IEEEWPDRAI IFANTKYKCE SIWAHLAADG HRVGLLTGDV PQKKREKILE
     QFTQGSVDLL VATDVAARGL HIPQVTHVFN YDLPDDCEDY VHRIGRTGRA GASGHSISFA
     CEDYAINLPA IEEYIEHTIP VSDYDSSALI QDLPAPVRTP SARNQQRRTN TGGARSGDRK
     SNNRRPRQPR QHKEA