ID   RAPA_PASMU              Reviewed;         967 AA.
AC   Q9CK01;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 118.
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=PM1837;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK03921.1; -; Genomic_DNA.
DR   RefSeq; WP_010907370.1; NC_002663.1.
DR   AlphaFoldDB; Q9CK01; -.
DR   SMR; Q9CK01; -.
DR   STRING; 747.DR93_96; -.
DR   EnsemblBacteria; AAK03921; AAK03921; PM1837.
DR   KEGG; pmu:PM1837; -.
DR   PATRIC; fig|272843.6.peg.1861; -.
DR   HOGENOM; CLU_011520_0_0_6; -.
DR   OMA; MSILERD; -.
DR   Proteomes; UP000000809; 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; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..967
FT                   /note="RNA polymerase-associated protein RapA"
FT                   /id="PRO_0000207178"
FT   DOMAIN          163..337
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   DOMAIN          489..660
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   MOTIF           283..286
FT                   /note="DEAH box"
FT   BINDING         176..183
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
SQ   SEQUENCE   967 AA;  109972 MW;  4919B77DAFB8E7BD CRC64;
     MTFAVGQRWM SESENNLGLG LIVAIDRRTV TILFPASEEQ RIYALNSAPL TRVLFQIGDE
     IAHHEGWKGN VLDILENNGV AFYLLKRQDN GEEITIQERD IAHQMTFSKP QDRLFTTQID
     RNEHFTLRYQ ALTHQQAQFQ SPLRGLRGIR AGLIPHQLHI AREVGQRTAP RVLLADEVGL
     GKTIEAGMIL QQQLFAEKVE RVLIIVPETL QHQWLVEMLR RFNLHFALFD EERCADFEDP
     ASALWINPFN TESQIICALD WLCEKPKRVE QLLEAGFDML IVDEAHHLGW SEHNPSLEYQ
     LVEQLARQIP AVLLLTATPE QLGQESHFAR LSLLDPDRFY DYQAFVQEQQ QYQPVAEAVQ
     SLLADKPLSA VEKNHISDLL SEQDVEPLLK VLDSQAHDEQ KALARQELID NLIDRHGTSR
     VLFRNTRQGV KGFPHRTYNQ ITLELPKQYN NAANVLAMLG EKGDNDSFYP EQMFQKLNPD
     ARWWEFDPRL EWLITFLKNH REEKVLVICR HANTAIQLEQ ALREKEAIRA AVFHEKLSIV
     ERDRAAAYFA QQEDGAQLLL SSSIGSEGRN FQFASHLVLF NLPDDPDLLE QCIGRLDRIG
     QRRDIQIHVP CFADTAQVVL ARWYHEGLNA FEETCPMGMT LFEAHQTQLN KFLQNPTALE
     GFAEFVSLTR KQQHELKQAL EKGRDRLLEL NSNGGEQAQQ LATDIAEQDG TTELVNFTLN
     LFDIIGVDQE DLGEKSIVIT LASNMLVPDF PGLKEEGATV TFDRQLSLAR EDVEFISWDH
     PLIRHGIDLI TSGDIGKSAV SLLINKALPA GTLLLEMIYV VEAQAPKGLQ LTRFLPPTPI
     RLLLDQKGNN LAEQVSFSAL QKQLKPIGKN MANKVVKMVR PNIEQLVKLS EQKIVAQAQQ
     IIHNAQQLAD QTLSAELNRL TALQAVNKNI RQDEVDALDN IRSQSLAQLQ QATWRLDSLR
     VIVSNKE