ID RAPA_VIBVY Reviewed; 969 AA.
AC Q7MHE6;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 115.
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=VV2925;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000037; BAC95689.1; -; Genomic_DNA.
DR RefSeq; WP_011151234.1; NC_005139.1.
DR AlphaFoldDB; Q7MHE6; -.
DR SMR; Q7MHE6; -.
DR STRING; 672.VV93_v1c26480; -.
DR KEGG; vvy:VV2925; -.
DR PATRIC; fig|196600.6.peg.2906; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_011520_0_0_6; -.
DR Proteomes; UP000002675; 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 DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd18011; DEXDc_RapA; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 2.30.30.930; -; 1.
DR Gene3D; 3.30.360.80; -; 1.
DR Gene3D; 6.10.140.1500; -; 1.
DR Gene3D; 6.10.140.2230; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 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; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR040765; Tudor_1_RapA.
DR InterPro; IPR040766; Tudor_2_RapA.
DR PANTHER; PTHR45766; DNA ANNEALING HELICASE AND ENDONUCLEASE ZRANB3 FAMILY MEMBER; 1.
DR PANTHER; PTHR45766:SF3; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A-LIKE PROTEIN 1; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 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_0000207191"
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; 109275 MW; 7C2B1FE2582F1BEF CRC64;
MAFALGQRWI SDTESDLGLG TVVALDARTV TLMFAASEEN RVYASNDAPV TRVVFNVGDV
VECQEGWSLK VEQVVEENGL YTYLGMREDT EETGVALREI FLSNQIRFNK PQDKMYAGQI
DRMDNFVLRY RALKNQYEQH RSPMRGLCGM RAGLIPHQLY IAHEVGRRHA PRVLLADEVG
LGKTIEAGMI IHQQVLLGRA ERILIVVPET LQHQWLVEMM RRFNLHFSIF DEERCIEAFA
ESDNPFDTQQ YVLCSLDFLR KSRKRFEQAL EADWDLLVVD 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
NEALNDVIAE SAKLNQALKA DLEQGRDRLL EMHSNGGEKA QQIVAEIAAK DGDTNLVSFA
LSLFDTIGLN QDDKGENAIV VTPSEHMMVP SYPGLPYEGA TITFDRDTAL SREDMHFISW
EHPMIQGGID LLMSEGVGTC AVSLLKNKAL PVGTLLLELI YAVDAQAPKR SGIGRFLPRT
PIRLMMDARG NDLSAQVEFE SFNRQLSPVN RHLASKLVSS VQNDIHRLIE AGDQLVVENV
EAIRQQAQQE MQQSLNSELE RLQALKAVNP NIRDEEIEAI DAQIKELNGY IAKAQFQLDS
LRLIVVSHN
//
