ID   RAPA_HISS2              Reviewed;         966 AA.
AC   B0URM0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=HSM_0458;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-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; CP000947; ACA32102.1; -; Genomic_DNA.
DR   RefSeq; WP_012341296.1; NC_010519.1.
DR   AlphaFoldDB; B0URM0; -.
DR   SMR; B0URM0; -.
DR   STRING; 228400.HSM_0458; -.
DR   EnsemblBacteria; ACA32102; ACA32102; HSM_0458.
DR   KEGG; hsm:HSM_0458; -.
DR   HOGENOM; CLU_011520_0_0_6; -.
DR   OMA; MSILERD; -.
DR   OrthoDB; 291634at2; -.
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_1000088362"
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;  110170 MW;  6C18FB54CB89AFDA CRC64;
     MLFAIGQRWI SESENSLGLG IITGQDNRTV TISFPASDEI RIYALASAPL TRVLFQKGDE
     ITHQLGWKAK VVDVMIRNEL AFYLVQRLDN NEEIAVQEME 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 NAINVLKMLG EIKDPELFYP EQIFQKMNAD
     ATWWRFDPRV DWLIHLVKSL REEKILVICQ DAITATQLEQ ALREKEGIRS AVFHENMSII
     ERDRASAYFA QQEEGAQVLL SSSIGSEGRN FQFACHLVLF HLPNNPDLLE QCIGRLDRIG
     QRRDIQIYVP CFADTPQIRL AQWYHEGLNA FEETCPMGAI LHEKCGAKLT EFLTSDTTDD
     FQSFIQQTHQ QQLQLKSELE QGRDRLLELN SNGGIQAQQL ANDIAIQDGS TELIDFTLNL
     FDIIGVEQED LGEKSIVISP TGTMLVPDFP GLKEEGVTVT FDRDLALARE ELEFLTWDHP
     IVRNGIDLIV SGDIGKSAVA LLVNKQLPTG TLLLELVYII ESQSPRGLQL TRFLPPTPLR
     LLLDIKGNDL SHQISFQGLQ KQLKPMGKNM ATKVIKIMRP AIEQLIKQSE KNVVEPAKMI
     IEQAKQLADQ SLSAEINRLY ALQAVNKNIR PEEIEQLESQ RTLSLELLNQ ANWRLDSLRV
     IVSNKE