ID RAPA_PSEAE Reviewed; 950 AA.
AC Q9HYT6;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 125.
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=PA3308;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG06696.1; -; Genomic_DNA.
DR PIR; G83231; G83231.
DR RefSeq; NP_251998.1; NC_002516.2.
DR RefSeq; WP_003119658.1; NC_002516.2.
DR AlphaFoldDB; Q9HYT6; -.
DR SMR; Q9HYT6; -.
DR STRING; 208964.PA3308; -.
DR PaxDb; 208964-PA3308; -.
DR GeneID; 882473; -.
DR KEGG; pae:PA3308; -.
DR PATRIC; fig|208964.12.peg.3464; -.
DR PseudoCAP; PA3308; -.
DR HOGENOM; CLU_011520_0_0_6; -.
DR InParanoid; Q9HYT6; -.
DR OrthoDB; 9814088at2; -.
DR PhylomeDB; Q9HYT6; -.
DR BioCyc; PAER208964:G1FZ6-3372-MONOMER; -.
DR Proteomes; UP000002438; 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 DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd18011; DEXDc_RapA; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 2.30.30.930; -; 1.
DR Gene3D; 3.30.360.80; -; 1.
DR Gene3D; 6.10.140.1500; -; 1.
DR Gene3D; 6.10.140.2230; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 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; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR040765; Tudor_1_RapA.
DR InterPro; IPR040766; Tudor_2_RapA.
DR PANTHER; PTHR45766; DNA ANNEALING HELICASE AND ENDONUCLEASE ZRANB3 FAMILY MEMBER; 1.
DR PANTHER; PTHR45766:SF3; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A-LIKE PROTEIN 1; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 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..950
FT /note="RNA polymerase-associated protein RapA"
FT /id="PRO_0000207181"
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; 106872 MW; 26911065FD197FCE CRC64;
MDMAQYQPGQ RWISDSEAEL GLGTILAQDG RLLTVLYPAT GDTRQYALRN APLTRVRFAP
GDEVTHFEGW KMTVREVEES EGLLVYHGLT AQNEQRTLPE 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
//
