RAPA_SHEON
ID RAPA_SHEON Reviewed; 968 AA.
AC Q8EJ93;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=SO_0575;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(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; AE014299; AAN53655.1; -; Genomic_DNA.
DR RefSeq; NP_716210.1; NC_004347.2.
DR RefSeq; WP_011070913.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EJ93; -.
DR SMR; Q8EJ93; -.
DR STRING; 211586.SO_0575; -.
DR PaxDb; Q8EJ93; -.
DR KEGG; son:SO_0575; -.
DR PATRIC; fig|211586.12.peg.555; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OMA; MSILERD; -.
DR OrthoDB; 291634at2; -.
DR PhylomeDB; Q8EJ93; -.
DR BioCyc; SONE211586:G1GMP-545-MON; -.
DR Proteomes; UP000008186; 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..968
FT /note="RNA polymerase-associated protein RapA"
FT /id="PRO_0000207186"
FT DOMAIN 163..332
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT DOMAIN 491..655
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT MOTIF 278..281
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 968 AA; 109262 MW; 543F47B925E5D713 CRC64;
MPFALGQRWI SDTESELGLG TVVQVEGRMV TVLFPATGEN RMFSRNEAPL TRVIYNPGDT
VESHEGWSLS VEELTEKDDL VVYHGIHSET GEKVSLRETL LNHNIRFNKP QDRLFAGQID
RLDRFGIRYQ CQLLRHQLAT SDLLGLQGPR VGLIPHQMWI AHEVGRRYAP RVLLADEVGL
GKTIEAGLII HQQLLTCRAE RVLIIVPDTL RHQWLVEMLR RFNLRFSVFD EDRCVEAFAD
HDNPFYTEQL VICSLELLRK KKRLDQALDA DWDLLVVDEA HHLEWTEEAP SRAYQVVEAL
SEVVPGVLLL TATPDQLGHE SHFARLRLLD PDRFYDYDAF LAEENSYKDV AIAAEALAGE
SKLSDYAINS LTELLSEKDI APSIRLIQAE GIDSELQQAA RSELLQELLD RHGTGRVLYR
NSRASVKGFP KRIFNAYPHA MPEQYLTAAR VNDMMGGRKS LEAKAAQALS PEKLYQEFED
NSASWWKFDP RVDWLIEFLK SHRSKKVLII ASGADTALSL EEALRTREGI QATVFHEGMS
IIERDKAGAY FAQEEGGAQA LICSEIGSEG RNFQFASHLV LFDLPLNPDL LEQRIGRLDR
IGQKNDIQIH LPYLQDTAQE RLLQWYHQGL NAFELTCPGG HILFSEFAEE LLNVLVGGDE
DELTNLLNHT QSRYKELKHA MEQGRDKLLE INSHGGDKAK AIVERLAQSD QDTKLIGSVI
RLWDIIGVDQ EDKGENSIIL RPSEHMMFPT YPGLHEDGVT VTFDRDTALS RDDIALITQE
HPLVQTGLDL ITGSDTGTTS VAILKNKALP AGTLFLELIY MADASAPKSS QLYRYLPPTP
IRILLDKNGN DLSAKVDYTS FDKQLSAVNR HIGSKLVTAS QPILHPLFAK GEEYAQVAVN
ELVAQAREKM TSQLTGELER LESLKAVNPN IREEELEYLR NQMQELTTYL DASQLQLDAI
RMVLVSHV
