ID   RAPA_HAEI8              Reviewed;         923 AA.
AC   Q4QMI0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=NTHI0873;
OS   Haemophilus influenzae (strain 86-028NP).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=281310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=86-028NP;
RX   PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA   Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA   Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA   Munson R.S. Jr.;
RT   "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT   influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL   J. Bacteriol. 187:4627-4636(2005).
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; CP000057; AAX87767.1; -; Genomic_DNA.
DR   RefSeq; WP_011272194.1; NC_007146.2.
DR   AlphaFoldDB; Q4QMI0; -.
DR   SMR; Q4QMI0; -.
DR   PRIDE; Q4QMI0; -.
DR   EnsemblBacteria; AAX87767; AAX87767; NTHI0873.
DR   KEGG; hit:NTHI0873; -.
DR   HOGENOM; CLU_011520_0_0_6; -.
DR   OMA; MSILERD; -.
DR   OrthoDB; 291634at2; -.
DR   Proteomes; UP000002525; 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..923
FT                   /note="RNA polymerase-associated protein RapA"
FT                   /id="PRO_1000088359"
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;  104415 MW;  637B44770A70D487 CRC64;
     MPFAIGQRWL SESENALGLG VITALDQRTV TIYFPAADET RIYAAAQAPL SRIVFSKGET
     LSHQAGWQGE ILDVQNMNGL LFYLVKTPQD EDVIVQERDI SPIISFSQAK DRLFSAQIDR
     SSHFALRYRT LCHQQAQFKS PLRGLRGTRA GLIPHQLHIA AEVGNRVNPR VLLADEVGLG
     KTIEAGMILQ NQLFAEKVQR VLIIVPETLQ HQWLVEMLRR FNLHFSLFDE ERCNDFDLDA
     VNPFMTESLI ICSLNWLETH PNRVEQALDA QFDCLIVDEA HHLVWSESAP SAAYLLVEQL
     ARIIPSVLLL TATPEQLGQE SHFARLRLLD PERFFDYQTF VKEQKRYQPV VNAIESLLAN
     KALSAVEKNH ISDLLLEQDV EPLFKAIASN NDEEQHRARQ ELIQALIDRH GTGRMLFRNT
     RQGVKGFPHR VYHQITLSEE NDKIDWLINF LKLHRDEKIF VICQTAATAI QLEQILRERE
     AIRAAVFHEK MSIIERDRAA AYFADLENGA QVLLSSSIGS EGRNFQFAAN LVLFDLPTNP
     DLLEQCIGRL DRIGQKRDVQ IYVPCAKDSP QIRLARWYNE GLNAFEQTCP MGMALFSQFE
     DELEKVRSNS TALSENEFSE LLKQTKTVRE KLKIELEKGR DRLLELNSNG GKQAQALADQ
     IADEDNSPEL VNFALKLFDI IGVEQEDLGA NSIVISPTGT MLVPDFPGLK EEGVTVTFDR
     ELALAREEME FLTWDHPMIR QGIDLVASGD IGKAAMALLV NKQLPAGTLL IELIYIVESQ
     SPKGLQLNRF LPPTPIRLLL DNKGNNIGEQ VAFETLHSKL KPLGKNIANQ MVKMARGNIE
     ALITRGDQLV KSLAEPIITE AKNQADQQLS AEINRLQALR AVNQNIRQSE IDILEQQRTQ
     SLDELSKANW RLDCLRVIVT NKE