ID   RAPA_PSEA8              Reviewed;         950 AA.
AC   B7V6T4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=PLES_17581;
OS   Pseudomonas aeruginosa (strain LESB58).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=557722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LESB58;
RX   PubMed=19047519; DOI=10.1101/gr.086082.108;
RA   Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I.,
RA   Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A.,
RA   Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D.,
RA   Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.;
RT   "Newly introduced genomic prophage islands are critical determinants of in
RT   vivo competitiveness in the Liverpool epidemic strain of Pseudomonas
RT   aeruginosa.";
RL   Genome Res. 19:12-23(2009).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FM209186; CAW26486.1; -; Genomic_DNA.
DR   AlphaFoldDB; B7V6T4; -.
DR   SMR; B7V6T4; -.
DR   KEGG; pag:PLES_17581; -.
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..950
FT                   /note="RNA polymerase-associated protein RapA"
FT                   /id="PRO_1000188181"
FT   DOMAIN          165..333
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   DOMAIN          475..629
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   MOTIF           279..282
FT                   /note="DEAH box"
FT   BINDING         178..185
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
SQ   SEQUENCE   950 AA;  106819 MW;  A104C3CC2F7618EA CRC64;
     MDMAQYQPGQ RWISDSEAEL GLGTILAQDG RLLTVLYPAT GDTRQYALRN APLTRVRFAP
     GDEVTHFEGW KMTVREVEES EGLLVYHGLT AQNEQCTLPE TQLSNFIQFR LASDRLFAGQ
     IDPLPWFSLR YHTLERRSQL LQSSLWGLGG ARAQPIAHQL HIAREVADRM APRVLLADEV
     GLGKTIEAGL IIHRQLLSGR AGRVLILVPE NLQHQWLVEM RRRFNLQVAL FDKERFAESD
     ASNPFEDTQL ALVALEWLKE DERAQDALFA AGWDLLVVDE AHHLVWHQDQ VSAEYALVEQ
     LAEIIPGVLL LTATPEQLGQ DSHFARLRLL DPNRFHDLEA FRRESEQYRP VAEAVQELLD
     HGSLSAGARK AIHGFLGSEG DELLASVEGG DEEARSRLVR ELLDRHGTGR VLFRNTRAAV
     QGFPQRELHA YPLPMPSQYE ELPAGEHPDL YPEVNFQQQW EDGDDNNRWW RFDPRVEWLI
     DTLKMLKQFK VLVICAHAET ALDLEDALRL RSGISATVFH EGMSILERDR AAAYFADEEF
     GAQVLICSEI GSEGRNFQFA HHLVLFDLPA HPDLLEQRIG RLDRIGQRHT IQLHVPHLEN
     SAQQRLFQWY HQALNAFLNT CPTGNALQHE FGPRLLPLLD GGEDKAWDAL LAEGRARREA
     LEAELHSGRD RLLELNSGGA GEGEALVEAI EEQDDDFALP IYMERLFDAY GIHSEDHSEN
     ALILKPSEKM LDAGFPLGDD EGVTITYDRA QALAREDMQF LTWEHPMVQG GMDLVLSGSM
     GNTSVALIKN KALKPGTVLL ELLFVSEAVA PRALQLGRWL PPQALRCLLD ANGNDLAGRV
     SLETLNDQLE SVPRVSANKF VQAQRDVLAK QFDVAEGKIV PRHEERVARA KQQFAAAMDE
     ELARLTALKA VNPSVRDSEL DSLRTQREEG LALLDKASLR LEAIRILVAG