RAPA_PSEU2
ID RAPA_PSEU2 Reviewed; 948 AA.
AC Q4ZPQ0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=Psyr_3842;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY38872.1; -; Genomic_DNA.
DR RefSeq; WP_011268689.1; NC_007005.1.
DR RefSeq; YP_236910.1; NC_007005.1.
DR AlphaFoldDB; Q4ZPQ0; -.
DR SMR; Q4ZPQ0; -.
DR STRING; 205918.Psyr_3842; -.
DR EnsemblBacteria; AAY38872; AAY38872; Psyr_3842.
DR KEGG; psb:Psyr_3842; -.
DR PATRIC; fig|205918.7.peg.3948; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OMA; MSILERD; -.
DR Proteomes; UP000000426; 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_1000088370"
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; 106664 MW; 45785E953E0FFD2A CRC64;
MAQQYQPGQR WISDSEAELG LGTVLAQDGR LLTVLYPATG ETRQYALRNA PLTRVRFSPG
DVITHFENWK MTVREVDDVD GLLVYHGLNA QNELVTLPET QLSNFIQFRL ATDRLFAGQI
DQLSWFSLRY NTLEHTSRQL QSSLWGLGGV RAQPIAHQLH IAREVADRIA PRVLLADEVG
LGKTIEAGLV IHRQLLSGRA SRVLILVPEN LQHQWLVEMR RRFNLQVALF DAERFMESDA
GNPFEDTQLA LVALEWLVED EKAQDALFAA GWDLMVVDEA HHLVWHEDKA SREYSLVEQL
AEVIAGVLLL TATPEQLGQD SHFARLRLLD PNRFHDLKAF RAESENYRPV AQAVQELLDK
GKLSAAAQET IHGFLGAEGD SLLAAVNTGD EEAKSRLIRE LLDRHGTGRV LFRNTRAAVQ
GFPERKLHQY PLPCPVEYLE LPVGEHADLY PEVSFQSHSD VSEEERWWRF DPRVDWLIDT
LKMLKRVKVL VICAHAETAM DLEDALRVRS GIPATVFHEG MNILERDRAA AYFADEEFGA
QVLICSEIGS EGRNFQFSHH LVLFDLPSHP DLLEQRIGRL DRIGQKHTIE LHVPFLETSP
QARLFQWYHE ALNAFLNTCP TGNALQHQFG PRLLPLLESG DDDKWQTLIN EARSERERLE
SELHTGRDRL LELNSGGAGE GEALVEAILD QDDQFSLPIY METLFDAFGI DSEDHSENAL
ILKPSEKMLD ASFPLGDDEG VTITYDRNQA LSREDMQFIT WEHPMVQGGM DLVLSGSMGN
TAVALIKNKA LKPGTVLLEL IYVSEVVAPR SLQLGRYLPP AALRCLLDPN GNDLASRVSF
NTLNDQLESV PRASANKFIQ AQRDQLTPRI NAGEEKIMPK HAERVAEAQR RLAADTEEEL
ARLTALQAVN PTVRDSELVA LRTQREQGLA MLEKAALRLE AIRVLVAG