RAPA_PSESM
ID RAPA_PSESM Reviewed; 948 AA.
AC Q87XS2;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-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=PSPTO_4104;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO57560.1; -; Genomic_DNA.
DR RefSeq; NP_793865.1; NC_004578.1.
DR RefSeq; WP_005764946.1; NC_004578.1.
DR AlphaFoldDB; Q87XS2; -.
DR SMR; Q87XS2; -.
DR STRING; 223283.PSPTO_4104; -.
DR EnsemblBacteria; AAO57560; AAO57560; PSPTO_4104.
DR GeneID; 1185784; -.
DR KEGG; pst:PSPTO_4104; -.
DR PATRIC; fig|223283.9.peg.4210; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OMA; MSILERD; -.
DR OrthoDB; 291634at2; -.
DR PhylomeDB; Q87XS2; -.
DR Proteomes; UP000002515; 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_0000207183"
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; 106625 MW; 81E4A771C9286C4D CRC64;
MAQQYQPGQR WISDSEAELG LGTVLAQDGR LLTVLYPATG ETRQYALRNA PLTRVRFSPG
DVITHFENWK MTVREVDDVD GLLVYHGLNA QNEVVTLPET QLSNFIQFRL ATDRLFAGQI
DQLSWFSLRY NTLEHTSRQL QSSLWGLGGV RAQPIAHQLH IAREVADRIA PRVLLADEVG
LGKTIEAGLV IHRQLLSGRA NRVLILVPEN LQHQWLVEMR RRFNLQVALF DAERFMESDA
GNPFEDTQLA LVALEWLVED EKAQDALFAA GWDLMVVDEA HHLVWHEEKA SREYSLVEQL
AEVIAGVLLL TATPEQLGQD SHFARLRLLD PNRFHDLKAF RAESENYRPV AQAVQELLDK
GKLSAAAQKT IHGFLGAEGD TLLAAVNAGD DEAKARLIRE LLDRHGTGRV LFRNTRAAVQ
GFPERKLHQY PLPCPVEYLE LPVGEHADLY PEVSFQSQSD ASEEERWWRF DPRVEWLIDT
LKMLKRVKVL VICAHAETAM DLEDALRVRS GIPATVFHEG MNILERDRAA AYFADEEFGA
QVLICSEIGS EGRNFQFSHH LVLFDLPSHP DLLEQRIGRL DRIGQKHVIE LHVPFLETSP
QARLFQWYHE ALNAFLNTCP TGNALQHQFG PRLLPLLESG DDDEWQSLID EARSERERLE
SELHTGRDRL LELNSGGAGE GEALVEDILE QDDQFSLPIY METLFDAFGI DSEDHSENAL
ILKPSEKMLD ASFPLGDDEG VTITYDRNQA LSREDMQFIT WEHPMVQGGM DLVLSGSMGN
TAVALIKNKA LKPGTVLLEL IYVSEVVAPR SLQLGRYLPP AALRCLLDAN GNDLSSRVSF
NTLNDQLESV PRASANKFIQ AQRDQLTPRI NAGEEKITPK HAERVAEAQR RLAADTEEEL
ARLTALQAVN PTVRDSELVA LRTQREQGLA MLEKAALRLE AIRVLVAG
