ID   RAPA_HAES1              Reviewed;         966 AA.
AC   Q0I5G1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=HS_1516;
OS   Haemophilus somnus (strain 129Pt) (Histophilus somni).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=205914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129Pt;
RX   PubMed=17172329; DOI=10.1128/jb.01422-06;
RA   Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA   Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA   Xie G., Inzana T.J.;
RT   "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain
RT   129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus
RT   influenzae Rd.";
RL   J. Bacteriol. 189:1890-1898(2007).
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; CP000436; ABI25789.1; -; Genomic_DNA.
DR   RefSeq; WP_011609667.1; NC_008309.1.
DR   AlphaFoldDB; Q0I5G1; -.
DR   SMR; Q0I5G1; -.
DR   STRING; 205914.HS_1516; -.
DR   EnsemblBacteria; ABI25789; ABI25789; HS_1516.
DR   KEGG; hso:HS_1516; -.
DR   eggNOG; COG0553; Bacteria.
DR   HOGENOM; CLU_011520_0_0_6; -.
DR   OMA; MSILERD; -.
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..966
FT                   /note="RNA polymerase-associated protein RapA"
FT                   /id="PRO_1000088361"
FT   DOMAIN          163..337
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   DOMAIN          489..643
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   966 AA;  110135 MW;  88067732CDBD0056 CRC64;
     MLFAIGQRWI SESENSLGLG IITGQDNRTV TISFPASDET RIYALASAPL TRVLFQKGDE
     ITHQLGWKAR VVDVMMRNEL AFYLVQRLDN NEEIVVQEME LAHQISFSKP QDRLFSTQID
     RNEHFVLRYK ALKHQQEQFQ SSLRGLRGNR AGLIPHQLHI AQEVGRRIAP RVLLADEVGL
     GKTIEAGMIL QQQLLAEKVQ RVLILVPETL QHQWLVEMLR RFNLHFSLFD EERCADFDNP
     EDHVEANPFV AENLIICALD WLVQQPKRAK QALAGEFDLL IVDEAHHLTW SEDSPSIAYE
     LVMQLSAVIP AVLLLTATPE QLGQQSHFAR LHLLDPNRFY SYRAFEKEQQ QYQPVAKAVQ
     SLLSEHILTV EEQNHLAELL SEQDIEPMLK VINSQADTEQ KQVARGELMS NLIDRHGTGR
     LLFRNTRQGV QGFPHRIYHQ IKLDLPTQYQ NAINVLNMLG EIKDPELFYP EQIFQKMNAD
     ATWWRFDPRV DWLINLVKSL REEKILVICQ DAITAIQLEQ ALREKEGIRS AVFHENMSII
     ERDRASAYFA QQEEGAQVLL SSSIGSEGRN FQFACHLVLF HLPNNPDLLE QCIGRLDRIG
     QRRDIQIYVP CFADTPQIRL AQWYHEGLNA FEETCPMGAI LHEKCGAKLT EFLTSDTTDD
     FQAFIQQTHQ QQLQLKSELE QGRDRLLELN SNGGEQAQQL ANDIAIQDGS TELIDFTLNL
     FDIIGVEQED LGEKSIVISP TGTMLVPDFP GLKEEGVTVT FDRDLALARE DLEFLTWDHP
     IVRNGIDLIV SGDIGKSAVA LLVNKQLPTG TLLLELVYII ESQSPRGLQL TRFLPPTPLR
     LLLDIKGNDL SHQISFQGLQ KQLKPMGKNM ATKVIKIMRP AIEQLIKQSA KNVVEPAKMI
     IEQAKQLADQ SLSAEINRLY ALQAVNKNIR PEEIEQLESQ RTLSLELLNQ ANWRLDSLRV
     IVSNKE