RAPA_PSEPK
ID RAPA_PSEPK Reviewed; 948 AA.
AC Q88NR0;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=PP_1145;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN66770.1; -; Genomic_DNA.
DR RefSeq; NP_743306.1; NC_002947.4.
DR RefSeq; WP_010952303.1; NC_002947.4.
DR AlphaFoldDB; Q88NR0; -.
DR SMR; Q88NR0; -.
DR STRING; 160488.PP_1145; -.
DR EnsemblBacteria; AAN66770; AAN66770; PP_1145.
DR KEGG; ppu:PP_1145; -.
DR PATRIC; fig|160488.4.peg.1215; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OMA; MSILERD; -.
DR PhylomeDB; Q88NR0; -.
DR BioCyc; PPUT160488:G1G01-1223-MON; -.
DR Proteomes; UP000000556; 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..948
FT /note="RNA polymerase-associated protein RapA"
FT /id="PRO_0000207182"
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; 105995 MW; 8BAEAE86BCA71D0C CRC64;
MAQQYQPGQR WISDSEAELG LGTILAQDGR LLTVLYPATG DTRQYSLRNA PLTRVRFSPG
DQITHFEGWK LTVREVEDID GLMVYHGLDG QNQPRTLPET QLSNFIQFRL ASDRLFAGQI
DPLSWFSLRY NTLQHTSKQM QSALWGLGGC RAQPIAHQLH IAREVADRSA PRVLLADEVG
LGKTIEAGLV IHRQLLSGRA SRVLILVPEN LQHQWLVEMR RRFNLQVALF DAERFIESDA
SNPFEDAQLA LVALEWLVDD EKAQDALFAA GWDLLVVDEA HHLVWHEDQV SAEYGLVEQL
AQVIPGVLLL TATPEQLGQD SHFARLRLLD PNRFHDLAAF RAESEHYRPV AEAVQELLDE
GRLSPKAHAT ILGFLGAEGE ALLAAVSDGD TQASARLIRE LLDRHGTGRV LFRNTRAAIQ
GFPERQLHPY PLPTPEQYRD LPAGEHAELY PEVAFQAQGE VADDERWWRF DPRVDWLIDT
LKMLKRTKVL VICAHAETAM DLEDALRVRS GIPASVFHEG MSILERDRAA AYFADEEFGA
QVLICSEIGS EGRNFQFAHH LVMFDLPAHP DLLEQRIGRL DRIGQKHTIQ LHIPYLQDSP
QERLFQWYHE GLNAFLNTCP TGNALQHQFG PRLLPLLEGG ENKAWDTLVA DARSERERLE
AELHTGRDRL LELNSGGAGE GQALVEAILE QDDQFALPIY METLFDAFGI DSEDHSENAL
ILKPSEKMLD ASFPLGDDEG VTITYDRGQA LSREDMQFLT WEHPMVQGGM DLVLSGSMGN
TAVALIKNKA LKPGTVLLEL LFVSEVVAPR SLQLGRYLPP AALRCLLDAN GNDLASRVAF
ETLNDQLESV PRASANKFVQ AQRDVLAKRI SGGEEKILPA HNERVAEAQR RLAAEADEEL
ARLVALQAVN PSVRDSEIDA LRKRREDGLA MLEKAALRLE AIRVLVAG
