ID   RAPA_VIBA3              Reviewed;         969 AA.
AC   B7VIC2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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}; OrderedLocusNames=VS_0350;
OS   Vibrio atlanticus (strain LGP32) (Vibrio splendidus (strain Mel32)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=575788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LGP32;
RA   Mazel D., Le Roux F.;
RT   "Vibrio splendidus str. LGP32 complete genome.";
RL   Submitted (FEB-2009) 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; FM954972; CAV17359.1; -; Genomic_DNA.
DR   RefSeq; WP_012603152.1; NC_011753.2.
DR   AlphaFoldDB; B7VIC2; -.
DR   SMR; B7VIC2; -.
DR   STRING; 575788.VS_0350; -.
DR   EnsemblBacteria; CAV17359; CAV17359; VS_0350.
DR   KEGG; vsp:VS_0350; -.
DR   PATRIC; fig|575788.5.peg.1716; -.
DR   eggNOG; COG0553; Bacteria.
DR   HOGENOM; CLU_011520_0_0_6; -.
DR   OMA; MSILERD; -.
DR   OrthoDB; 291634at2; -.
DR   Proteomes; UP000009100; 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; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..969
FT                   /note="RNA polymerase-associated protein RapA"
FT                   /id="PRO_1000188197"
FT   DOMAIN          164..334
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   DOMAIN          492..679
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;  109501 MW;  87EBF9A3481B174D CRC64;
     MTFALGQRWI SDTESDLGLG TVVAMDARTV TVMFAASEEN RVYARTDAPV TRVAFNVGDV
     IECQEGWSLS VEEVIEDKGL LTYLGTREDT QETEVTLREI FLSNQIRFNK PQDKLYAGQI
     DRMDNFVLRY RALSNQYQQH KSPMRGLCGM RAGLIPHQLY IAHEVGRRHA PRVLLADEVG
     LGKTIEAGMI IHQQVLSGRA ERILIVVPET LQHQWLVEMM RRFNLHFSIF DEERCIESFA
     ESDNPFDTQQ YVLCSLDFLR KSRKRYEQAL EGEWDLLVVD EAHHLEWSQD KPSREYQVVE
     GLAENTSGVL LLTATPEQLG RESHFARLRL LDPDRFYDYE AFVEEEDQYA PVADAVTALF
     SGVKLENSAK NQITELLSEQ DVEPLFRVIE GDSSEEEQAL ARQELIDNLM DRHGTGRVLF
     RNTRAAIKGF PKRNVNLLPM DIPTQYTTSM RVSGMIGGKM APEARAMKML YPEEIFQEFE
     GEDSSWWQFD SRVNWLIEKI QDKRSEKILV IASRASTALQ LEQALREREG VRATVFHEGM
     SILERDKAAA YFAQEEGGAQ VLICSEIGSE GRNFQFANQL VMFDLPFNPD LLEQRIGRLD
     RIGQLRDIDI HVPYLKGTSQ AILARWFDEG LNAFAETCPT GRTVYDKYSD VLIEMLASGN
     TEQLDEVIEE SAKLNQSLKS DLEKGRDRLL EMHSNGGDKA HEIAEKIAST DGDTNLVTFA
     LSLFDTIGLN QDDKGENALV VTPSEHMMVP SYPGLPYEGA TITFDRETAL SREDMNFISW
     EHPMIQGGID LLLSEGVGAS AVSLLKNKAL PVGTILLELV YLVDAQAPKR SGISQFLPKT
     PIRLMMDGRG NDLSAQVEFD SFNRQLSPVN RHLASKLVNS VQGEIHKLIE AGETHVLPKV
     EEVRQQAQKD MQTNLNGELE RLQALKAVNP NIRDEELEVI EAQINELTGY ISKAQVQLDS
     LRLIVVSHN