ID   RAPA_HAEIE              Reviewed;         923 AA.
AC   A5UAT0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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};
GN   OrderedLocusNames=CGSHiEE_02060;
OS   Haemophilus influenzae (strain PittEE).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=374930;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PittEE;
RX   PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA   Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA   Ehrlich G.D.;
RT   "Characterization and modeling of the Haemophilus influenzae core and
RT   supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT   nontypeable strains.";
RL   Genome Biol. 8:R103.1-R103.18(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; CP000671; ABQ97881.1; -; Genomic_DNA.
DR   RefSeq; WP_011961774.1; NC_009566.1.
DR   AlphaFoldDB; A5UAT0; -.
DR   SMR; A5UAT0; -.
DR   KEGG; hip:CGSHiEE_02060; -.
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; 1.
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..923
FT                   /note="RNA polymerase-associated protein RapA"
FT                   /id="PRO_1000088360"
FT   DOMAIN          162..332
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   DOMAIN          443..597
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   MOTIF           278..281
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   923 AA;  104354 MW;  08F2D2940FD89537 CRC64;
     MPFAIGQRWL SESENALGLG VITALDQRTV TIYFPAADET RIYAIAQAPL SRIVFSKGET
     LSHQAGWQGE ILDVQNMNGL LFYLVKNPQD EDVIVQERDI SPIISFSQAK DRLFSAQIDR
     STHFALRYRT LCHQQAQFKS PLRGLRGTRA GLIPHQLHIA AEVGNRVNPR VLLADEVGLG
     KTIEAGMILQ NQLFAEKVQR VLIIVPETLQ HQWLVEMLRR FNLHFALFDE ERCNDFDLDA
     VNPFTTESLI ICSLNWLETH PNRVEQALDA QFDCLIVDEA HHLVWSETSP SAAYLFVEQL
     ARIIPSVLLL TATPEQLGQE SHFARLRLLD PERFFDYQTF VKEQEHYQPV VNAVESLLAN
     KALSAVEKNH ISDLLLEQDV EPLFKAIASN NDEEQQRARQ ELIQALIDRH GTGRMLFRNT
     RQGVKGFPHR VYHQITLSEE NDKIDWLIDF LKLHRDEKIF VICQTAATAI QLEQILRERE
     AIRAAVFHEK MSIIERDRAA AYFADLENGA QVLLSSSIGS EGRNFQFAAN LVLFDLPTNP
     DLLEQCIGRL DRIGQKRDVQ IYMPCAKDSP QSRLARWYNE GLNAFEQTCP MGMALFSQFA
     DELEKVRSNS TALSENEFSG LLKQTKTARE KLKIELEKGR DRLLELNSHG GEQAQALADQ
     IADEDNSPEL VNFALKLFDI IGVEQEDLGA NSIVISPTGT MLVPDFPGLK EEGVTVTFDR
     ELALAREEME FLTWDHPMIR QGIDLVASGD IGKAAMALLV NKQLPAGTLL IELIYVVESQ
     SPKGLQLNRF LPPTPIRLLL DNKGNNMGEQ VAFETLHSKL KPLGKNIANQ MVKMARSNIE
     SLITRGDQLV KSLAEPIIAE AKNQADQQLS AEINRLQALR AVNKNIRQSE IDILEQQRTQ
     SLDELSKANW RLDCLRVIVT NKE