RAPA_PSEPF
ID RAPA_PSEPF Reviewed; 948 AA.
AC Q3KGV8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=Pfl01_1255;
OS Pseudomonas fluorescens (strain Pf0-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=205922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pf0-1;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(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}.
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DR EMBL; CP000094; ABA72998.1; -; Genomic_DNA.
DR RefSeq; WP_011332809.1; NC_007492.2.
DR AlphaFoldDB; Q3KGV8; -.
DR SMR; Q3KGV8; -.
DR STRING; 205922.Pfl01_1255; -.
DR EnsemblBacteria; ABA72998; ABA72998; Pfl01_1255.
DR KEGG; pfo:Pfl01_1255; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OMA; MSILERD; -.
DR Proteomes; UP000002704; 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..948
FT /note="RNA polymerase-associated protein RapA"
FT /id="PRO_1000088368"
FT DOMAIN 164..332
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT DOMAIN 473..627
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT MOTIF 278..281
FT /note="DEAH box"
FT BINDING 177..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
SQ SEQUENCE 948 AA; 106595 MW; F699A529E802839E CRC64;
MAQQYQPGQR WISDSEAELG LGTVLAQDGR LLTVLYPATG ETRQYALRNA PLTRVRFSPG
DSITHFEGWK MTVQQVDDVD GLMVYHGLNA QNEAVTLPET QLSNFIQFRL ASDRLFAGQI
DPLAWFSLRY HTLEHTSRQL QSALWGLGGV RAQPIAHQLH IAREVADRIA PRVLLADEVG
LGKTIEAGLV IHRQLLSGRA NRVLILVPEN LQHQWLVEMR RRFNLQVALF DEERFIESDA
TNPFEDTQLA LVALEWLVDD EKAQDALFAA GWDLMVVDEA HHLVWHEDKV SPEYSLVEQL
AEVIPGVLLL TATPEQLGQD SHFARLRLLD PNRFHDLAAF RAESENYRPV AEAVQELLDK
GRLSPAAHKT IHGFLGNEGE ALLTAVNDGD TEASARLVRE LLDRHGTGRV LFRNTRAAVQ
GFPERKLHPY PLPCPDEYLE LPLGEHAELY PEVSFQAQPD ASEEERWWKF DPRVEWLIDQ
LKMLKRTKVL VICAHAETAM DLEDALRVRS GIPATVFHEG MNILERDRAA AYFADEEFGA
QVLICSEIGS EGRNFQFAHH LVLFDLPSHP DLLEQRIGRL DRIGQKHIIE LHVPYLETSP
QERLFQWYHE ALNAFLNTCP TGNALQHQFG PRLLPLLEEA DDGEWQALID EARTERERLE
AELHTGRDRL LELNSGGAGE GEALVEAILE QDDQFALPIY METLFDAFGI DSEDHSENAL
ILKPSEKMLD ASFPLGDDEG VTITYDRNQA LSREDMQFIT WEHPMVQGGM DLVLSGSMGN
TAVALIKNKA LKPGTVLLEL LYVSEVVAPR SLQLGRYLPP AALRCLLDAN GNDLSSRVAF
ETLNDQLESV PRASANKFIQ AQRDQLTPRI NAGEDKVTPR HAERVAEARR RLAADTDEEL
ARLTALQAVN PTVRDSELDA LRKQREQGLA MLDKAALRLE AIRVLVAG
