ID   RAPA_HAEDU              Reviewed;         973 AA.
AC   Q7VKV0;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=HD_1764;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) 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; AE017143; AAP96518.1; -; Genomic_DNA.
DR   RefSeq; WP_010945547.1; NC_002940.2.
DR   AlphaFoldDB; Q7VKV0; -.
DR   SMR; Q7VKV0; -.
DR   STRING; 233412.HD_1764; -.
DR   PRIDE; Q7VKV0; -.
DR   EnsemblBacteria; AAP96518; AAP96518; HD_1764.
DR   KEGG; hdu:HD_1764; -.
DR   eggNOG; COG0553; Bacteria.
DR   HOGENOM; CLU_011520_0_0_6; -.
DR   OMA; MSILERD; -.
DR   Proteomes; UP000001022; 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..973
FT                   /note="RNA polymerase-associated protein RapA"
FT                   /id="PRO_0000207176"
FT   DOMAIN          162..339
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   DOMAIN          496..672
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   MOTIF           285..288
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   973 AA;  110202 MW;  453EE1904CF96D3E CRC64;
     MFIIGQRWIS ESENNLGLGI VTARDNRTVT IRFPAAEEER IYALAVAPLI RVQFQKGDRI
     NCIDGWQLDV EDVLDNQGFV IYLGSRVDNG EQVALPEMQL DHKVSFSKPQ DRLFSAQIDR
     SDRFALRYRA LQHQQAQFQS PLRAMRGIRA SLIPHQLHIA KEVGQRVAPR VLLADEVGLG
     KTIEAGMILQ QQLFSGRVER VLVLVPESLQ HQWLVEMLRR FNLNFSLFDE ERCSDFDKTD
     EDGNDISENP FESEALVIAS IDWLEKATTR ATQVLLADWD LLIVDEAHHL VCSATESSQA
     YQFVARLAKK ITAVLLLTAT PEQLGLDSHF ARLALLDPDR FYDYATFIAE QKAYKPVADA
     VANLLNDKPL NDMAKNAIAE LLSEQDTEPM FKIINSEKSA ESDRLQVRQE LINALIDRHG
     TSRVLFRNTR QGVKGFPHRV YHQITLEMPD QYANALNVRA MMGSMEPQDH FYPERLYQCL
     NSQAPMGNRW EDFDPRIAWL MTFLKNHRDE KVLIICKQAE IAITLAQVLR EREAIRTAVF
     HEHMTIVERD RAAAYFAQIE EGAQVLISSS IGSEGRNFQF ARNLVLFNLP DNPDLLEQSI
     GRLDRIGQKN DIQIYVPCFK NSMQIVLAEW YHRGLNAFEE TCPMGSNLFA EFSETLQSFF
     NDPQATGFEE FIAKTSKRRQ QLKMELEQGR DRLLELNSNG GETAQALAEA IAQEDNNPHL
     VNFALNLFDI IGLEQEDLGE KLIALNPTGH MLVSDFPGLS EEGTTITFDR QLALMREEIE
     LLTWDHPMIR HGIDLITSGD IGKCAISLLI NKNLPAGTLL LEAIYVVEAQ APKSLNLTRF
     LPPTPVRVLL DSKGNDMASQ VAFTSLEKQL KPVNKQMANK IAKMAQTQIK KLIMLSEQKI
     ETKAQAIIIA AKQQADNVLS AELHRLTSLQ AVNKNIRADE IELLEHLKAE SLAQLTQANW
     RLDSLRVIVS NKA