ID   RAPA_VIBC1              Reviewed;         969 AA.
AC   A7MSB2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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};
GN   OrderedLocusNames=VIBHAR_03676;
OS   Vibrio campbellii (strain ATCC BAA-1116).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=2902295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1116 / BB120;
RG   The Vibrio harveyi Genome Sequencing Project;
RA   Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA   Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA   Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA   Wilson R.K.;
RL   Submitted (AUG-2007) 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; CP000789; ABU72590.1; -; Genomic_DNA.
DR   RefSeq; WP_012128985.1; NC_022269.1.
DR   AlphaFoldDB; A7MSB2; -.
DR   SMR; A7MSB2; -.
DR   EnsemblBacteria; ABU72590; ABU72590; VIBHAR_03676.
DR   KEGG; vha:VIBHAR_03676; -.
DR   PATRIC; fig|338187.25.peg.2559; -.
DR   OMA; MSILERD; -.
DR   OrthoDB; 291634at2; -.
DR   Proteomes; UP000008152; Chromosome I.
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_1000088398"
FT   DOMAIN          164..334
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   DOMAIN          492..646
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;  110001 MW;  02A186DAD3DBC252 CRC64;
     MTFALGQRWI SDTESDLGLG TVVAMDARTV TLMFAASEEN RVYARNDAPV TRVTFNVGDV
     IDCQEGWSLK VEEVLEDEGL YTYFGTREDT QETAIVLREI FLSNHIRFNK PQDKLYAGQI
     DRMDNFVLRY RALQNQFEQH KSPMRGLCGM RAGLIPHQLY IAHEVGRRHA PRVLLADEVG
     LGKTIEAGMI IHQQVLSGRA ERILIVVPET LQHQWLVEMM RRFNLHFSIF DEERCIEAFA
     EAENPFDTQQ YVLCSLDFLR KSRKRFEQAL EGEWDLLVVD EAHHLEWSQD KPSREYQVVE
     GLAERTAGVL LLTATPEQLG RESHFARLRL LDPDRFYDYD AFVEEEEQYA PVADAITSLF
     SGEKLPDEAK NQITELLSEQ DVEPLFRIIE SDSDEEAKAS ARQELIDNLM DRHGTGRVLF
     RNTRAAIKGF PKRNVHLMPM DIPQQYTTSM RVSGMIGGKM TPEARAVKNL YPEEIFQEFE
     GEDSSWWQFD SRVNWLLEKV KEKRSDKVLV IASRASTALQ LEQALREREG IRATVFHEGM
     SILERDKAAA YFAQEEGGAQ VLICSEIGSE GRNFQFANQL VMFDLPFNPD LLEQRIGRLD
     RIGQKRDIDI HVPYLKDTSQ AILARWFDEG LNAFAETCPT GRAVYDKYSD ALIEMLASGD
     VSNLDEVIEE SAKMNKELKS QLEQGRDRLL EMHSNGGEKA QQIVEKISST DGDTNLVTFA
     LSLFDTIGLN QDDKGENALV VTPSEHMMVP SYPGLPYEGA TITFDRDTAL SREDMHFISW
     EHPMIQGGID LLMSEGVGTS AVSLLKNKAL PVGTILLELV YAVDAQAPKR SGITRFLPKT
     PIRMMMDARG NDLSPQVEFE GFNRQLSPVN RHLGSKLVTS VQKDIHSLIE AGDALVEQKV
     EEVRKQAHQD MQQSLNAELE RLQALKAVNP NIRDEEIESI EEQIKELTGY INQAQVQLDS
     LRLIVVSHN