ID   RAPA_VIBVU              Reviewed;         969 AA.
AC   Q8DCG1;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=RNA polymerase-associated protein RapA {ECO:0000255|HAMAP-Rule:MF_01821};
DE            EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_01821};
DE   AltName: Full=ATP-dependent helicase HepA {ECO:0000255|HAMAP-Rule:MF_01821};
GN   Name=rapA {ECO:0000255|HAMAP-Rule:MF_01821}; Synonyms=hepA;
GN   OrderedLocusNames=VV1_1459;
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: Transcription regulator that activates transcription by
CC       stimulating RNA polymerase (RNAP) recycling in case of stress
CC       conditions such as supercoiled DNA or high salt concentrations.
CC       Probably acts by releasing the RNAP, when it is trapped or immobilized
CC       on tightly supercoiled DNA. Does not activate transcription on linear
CC       DNA. Probably not involved in DNA repair. {ECO:0000255|HAMAP-
CC       Rule:MF_01821}.
CC   -!- SUBUNIT: Interacts with the RNAP. Has a higher affinity for the core
CC       RNAP than for the holoenzyme. Its ATPase activity is stimulated by
CC       binding to RNAP. {ECO:0000255|HAMAP-Rule:MF_01821}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RapA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01821}.
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DR   EMBL; AE016795; AAO09899.1; -; Genomic_DNA.
DR   RefSeq; WP_011079417.1; NC_004459.3.
DR   AlphaFoldDB; Q8DCG1; -.
DR   SMR; Q8DCG1; -.
DR   PRIDE; Q8DCG1; -.
DR   EnsemblBacteria; AAO09899; AAO09899; VV1_1459.
DR   KEGG; vvu:VV1_1459; -.
DR   HOGENOM; CLU_011520_0_0_6; -.
DR   OMA; MSILERD; -.
DR   Proteomes; UP000002275; Chromosome 1.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01821; Helicase_RapA; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR023949; Helicase_RapA.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR022737; RapA_C.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR040765; Tudor_1_RapA.
DR   InterPro; IPR040766; Tudor_2_RapA.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF12137; RapA_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   Pfam; PF18339; Tudor_1_RapA; 1.
DR   Pfam; PF18337; Tudor_RapA; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   Activator; ATP-binding; DNA-binding; Helicase; Hydrolase;
KW   Nucleotide-binding; Transcription; Transcription regulation.
FT   CHAIN           1..969
FT                   /note="RNA polymerase-associated protein RapA"
FT                   /id="PRO_0000207190"
FT   DOMAIN          164..334
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   DOMAIN          492..668
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   MOTIF           280..283
FT                   /note="DEAH box"
FT   BINDING         177..184
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
SQ   SEQUENCE   969 AA;  109248 MW;  E7C9D0A0ECF772AD CRC64;
     MAFALGQRWI SDTESDLGLG TVVALDARTV TLMFAASEEN RVYASNDAPV TRVVFNVGDV
     VECQEGWSLK VEQVVEENGL YTYLGTREDT EETGVALREI FLSNQIRFNK PQDKMYAGQI
     DRMDNFVLRY RALKNQYEQH RSPMRGLCGM RAGLIPHQLY IAHEVGRRHA PRVLLADEVG
     LGKTIEAGMI IHQQVLLGRA ERILIVVPET LQHQWLVEMM RRFNLHFSIF DEERCVEAFA
     ESDNPFDTQQ YVLCSLDFLR KSRKRFEQAL EAEWDLLVVD EAHHLEWSQD KPSRGYQVVE
     GLAERTPGVL LLTATPEQLG RESHFARLRL LDSDRFYDYA AFVEEEAQYA PVADAITALF
     SGVKLADEAK NQITELLSEQ DVEPLFRIIE SNADEESKAI ARQELIDNLM DRHGTGRVLF
     RNTRAAIKGF PVRNVHLLPM PIPTQYTTSM RVSGMIGGKL APEARAMKNL YPEEIFQEFE
     GEESSWWQFD CRVNWLLEKL KAQRSEKVLV IASRASTALQ LEQALREREG IRATVFHEGM
     SILERDKAAA YFAQEEGGAQ VLICSEIGSE GRNFQFANQL VMFDLPFNPD LLEQRIGRLD
     RIGQKRDIDI HVPYLQGTAQ EVLARWFNEG LNAFAETCPT GRTVYDQVSD QLIEMLASGS
     NEALDDVIAE SAKLNQALKA DLEQGRDRLL EMHSNGGEKA QQIVAEIAAK DGDTNLVSFA
     LSLFDTIGLN QDDKGENAIV VTPSEHMMVP SYPGLPYEGA TITFDRDTAL SREDMHFISW
     EHPMIQGGID LLMSEGVGTC AVSLLKNKAL PVGTLLLELI YAVDAQAPKR SGIGRFLPRT
     PIRLMMDARG NDLSGQVEFE SFNRQLSPVN RHLASKLVSS VQNDIHRLIE AGDQLVVENV
     EAIRQQAQQE MQQSLNSELE RLQALKAVNP NIRDEEIEAI DAQIKELNGY ISKAQFQLDS
     LRLIVVSHN