ID   RAPA_ACTP7              Reviewed;         969 AA.
AC   B3H0F9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=APP7_0319;
OS   Actinobacillus pleuropneumoniae serotype 7 (strain AP76).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=537457;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP76;
RA   Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N.,
RA   Tegetmeyer H., Singh M., Gerlach G.F.;
RT   "Genome and proteome analysis of A. pleuropneumoniae serotype 7.";
RL   Submitted (JUN-2008) 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; CP001091; ACE60971.1; -; Genomic_DNA.
DR   RefSeq; WP_005616776.1; NC_010939.1.
DR   AlphaFoldDB; B3H0F9; -.
DR   SMR; B3H0F9; -.
DR   EnsemblBacteria; ACE60971; ACE60971; APP7_0319.
DR   KEGG; apa:APP7_0319; -.
DR   HOGENOM; CLU_011520_0_0_6; -.
DR   OMA; MSILERD; -.
DR   BioCyc; APLE537457:APP7_RS01640-MON; -.
DR   Proteomes; UP000001226; Chromosome.
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_1000188165"
FT   DOMAIN          162..339
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   DOMAIN          492..663
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   MOTIF           285..288
FT                   /note="DEAH box"
FT   BINDING         175..182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
SQ   SEQUENCE   969 AA;  109717 MW;  39BB5C4E088AED6F CRC64;
     MFVVGQRWIS ESENNLGLGI VTASDNRTVT IQFPAAEEER IYALSVAPLT RVQFQKGDRI
     NSVEGWQLDV EEVVENQGFI IYLGKRADSG EEAVLPEMQL DHKVSFSKPQ DRLFSAQIDR
     SDRFALRYRA LQHQQAQFQS PLRGMRGIRA SLIPHQLHIA KEVGQRVAPR VLLADEVGLG
     KTIEAGMILQ QQLFSGRVER VLVLVPESLQ HQWLVEMLRR FNLKFSLFDE ERCSDFDKAD
     EDGNDVSENP FDSEALVIAS IDWLESSPNR AKQVLASHWD MLIVDEAHHL AWSEDEPSVG
     YQFVERLSKQ TPAVLLLTAT PEQLGQESHF ARLALLDADR FYDYHSFIAE QKDYKPVADA
     VATLLNDKPL SHDEQNSIAE LLSEKDTEPM FKVINSEKSK ENDRLQVRQE LIRELIDRHG
     TSRVLFRNTR QGVKGFPHRV YHQITLEMPS QYTNALKVMG MMGGVTKDDQ LYPERLFQRM
     NPAAKWADFD PRIEWLITFL KNHRDEKILV ICKQADTAIA LEQILREREA IRSAVFHEKM
     SIVERDRASA YFAQMEEGAQ VLISSSIGSE GRNFQFASNL VLFNLPDNPD LLEQSIGRLD
     RIGQKNDIQI HVPCFENSMQ MVLATWYHQG LNAFEETCPM GAALFREFGE ELEGFLKNPQ
     AVGFDEFLVR TFKRQQQLKA ELEQGRDRLL ELNSNGGEVA QALAEAIAKE DNNPHLVNFA
     LSLFDVIGLE QEDLGEQSIV ISPTGHMLVP DFPGIAEDGT TVTFDRQLAL MREDVEFLTW
     DHPMIRNGID LITSGYIGKS AISLLINKNL PAGTLLLEAI YMVETQAPKG LNLTRFLPPT
     PVRILLDNKG NDMAAQVSFA GLEKQLKPLN KQMANKIAKM AQADIKKLIG ISEQKIAAKL
     PELIEKASQD ADSTLSAELH RLTSLQAVNK NIRSDEIEAL EQQRIESLKQ IALANWRLDS
     LRVIVSNKE