RAPA_PECAS
ID RAPA_PECAS Reviewed; 967 AA.
AC Q6D0E6;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=ECA3853;
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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; BX950851; CAG76751.1; -; Genomic_DNA.
DR RefSeq; WP_011095351.1; NC_004547.2.
DR AlphaFoldDB; Q6D0E6; -.
DR SMR; Q6D0E6; -.
DR STRING; 218491.ECA3853; -.
DR EnsemblBacteria; CAG76751; CAG76751; ECA3853.
DR GeneID; 57210471; -.
DR KEGG; eca:ECA3853; -.
DR PATRIC; fig|218491.5.peg.3908; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OMA; MSILERD; -.
DR OrthoDB; 291634at2; -.
DR Proteomes; UP000007966; 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..967
FT /note="RNA polymerase-associated protein RapA"
FT /id="PRO_0000207175"
FT DOMAIN 163..333
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT DOMAIN 489..677
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT MOTIF 279..282
FT /note="DEAH box"
FT BINDING 176..183
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
SQ SEQUENCE 967 AA; 109835 MW; 4503D8A937021555 CRC64;
MPFTLGQRWI SDTESELGLG TVVAVNTRMI TLLFPASGEN RLYSRSDAPI TRVMFNPGDT
VTSHEGWQLK IDDVREEKGL LVYCGQRLDD ETPAELREVF LDSKLTFNKP QDRLFAGQID
RMDRFALRYR ARKHQNEQAL QQWGGLRGMR ASLIPHQLHI AYEVGQRHAP RVLLADEVGL
GKTIEAGMII HQQLLAGRAS RVLIVVPETL QHQWLVEMLR RFNLLFSLFD DERYAEAKLD
SSNPFETEQL VICSLGFVQR SAQRFAQLVN TDWDLLVVDE AHHLVWSEES PSPEYQAIEA
LARATPAVLL LTATPEQLGQ QSHFARLRLL DPNRFHDYQE FVAEQQQYRP VADAVTLLLA
GEKAQAAELN VLSDLLGEQD IEPLLKSINS DSDDNQKARQ ELITMLMDRH GTSRVLFRNT
RQGVKGFPQR VLHQIRLPLP AQYQTAIKVS GIMNANKPLE TRARDMLYPE QIYQQLEGDD
ATWWNFDPRV EWLLNYLTTN RDEKVLVICA QAATALQLEQ VLRTREAIRA AVFHEGLSIL
ERDRAAAYFA SEEEGAQVLI CSEIGSEGRN FQFASHLVMF DLPFNPDLLE QRIGRLDRIG
QAKEIQVLVP YLENTAQALL VRWYHEGLDA FEHTCPTGRT IYDAHHAQLI ERLTTVGEQQ
GLDEFIHTCR QQHDSLKQQL EQGRDRLLEM HSNGGEQAQL LAQAIAEQDN DVNLVTFALN
LFDIVGINQE DRSDNLIILT PSDHMLVPDF PGLPQDGCTI TFDRDQALSR EDAQFISWEH
PLIRNGLDLV LSGDTGSCAV SLLKNKALPV GTLLAELVYV VEAQAPKHLQ LTRFLPPTPV
RLLMDRKGTN LAAQVEFESF NRQLNAVNRH TSSKLVNAVQ SDVHAMLQQA EALVETQARQ
LITEAQQQAD LQLRRELERL EALKAVNPNI REDELTALEN QREQVLSNLH EANWRLDAIR
LVVVTHQ
