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Database: UniProt
Entry: A1RFP5
LinkDB: A1RFP5
Original site: A1RFP5 
ID   RAPA_SHESW              Reviewed;         968 AA.
AC   A1RFP5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   31-JUL-2019, entry version 72.
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};
GN   OrderedLocusNames=Sputw3181_0639;
OS   Shewanella sp. (strain W3-18-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=351745;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W3-18-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of Shewanella sp. W3-18-1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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
CC       immobilized on tightly supercoiled DNA. Does not activate
CC       transcription on linear DNA. Probably not involved in DNA repair.
CC       {ECO:0000255|HAMAP-Rule:MF_01821}.
CC   -!- SUBUNIT: Interacts with the RNAP. Has a higher affinity for the
CC       core RNAP than for the holoenzyme. Its ATPase activity is
CC       stimulated by binding to RNAP. {ECO:0000255|HAMAP-Rule:MF_01821}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RapA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01821}.
DR   EMBL; CP000503; ABM23490.1; -; Genomic_DNA.
DR   RefSeq; WP_011788020.1; NC_008750.1.
DR   EnsemblBacteria; ABM23490; ABM23490; Sputw3181_0639.
DR   KEGG; shw:Sputw3181_0639; -.
DR   HOGENOM; HOG000218482; -.
DR   KO; K03580; -.
DR   OMA; MSILERD; -.
DR   BioCyc; SSP351745:G1G7O-670-MONOMER; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.10810; -; 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_N; 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    968       RNA polymerase-associated protein RapA.
FT                                /FTId=PRO_1000088391.
FT   DOMAIN      163    332       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01821}.
FT   DOMAIN      491    643       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_01821}.
FT   NP_BIND     176    183       ATP. {ECO:0000255|HAMAP-Rule:MF_01821}.
FT   MOTIF       278    281       DEAH box.
SQ   SEQUENCE   968 AA;  109022 MW;  9DA958A86CD7A827 CRC64;
     MPFALGQRWI SDTESELGLG TVVQVEGRMV TVLFPATGEN RMFSRAEAPL TRVTYNPGDT
     VESHEGWSLT IEDLTEKDGL VIYHGIHSET GEQVTLRETL LNHNIRFNKP QDRLFAGQID
     RLDRFGVRYQ CQMLRHKLAT SDLLGLQGPR VGLIPHQMWI AHEVGRRYAP RVLLADEVGL
     GKTIEAGLII HQQLLTGRAE RVLVIVPDTL RHQWLVEMLR RFNLRFSVFD EDRCVEAYAD
     HDNPFYTEQL VICSLELLRK KKRLDQALDA DWDLLVVDEA HHLEWTEEAP SRAYQVVEAL
     SEVVPGVLLL TATPDQLGHE SHFARLRLLD PDRFYDYDAF LAEENSYKDV AIAAEALAGN
     AKLPDAAINS LTELLSEKDI APSIRLIQAD GIDSDVQQAA RSELLQELLD RHGTGRVLYR
     NSRASVKGFP KRFFNPHPQT MPEQYLTAAR VSSMMGGHKT LEAKAAQALS PEKLYQEFED
     NSASWWKFDP RVDWLIAFLK SHRSKKVLII ASQAETALSL EEALRTREGI QATVFHEGMS
     IIERDKAGAY FAQEEGGAQA LICSEIGSEG RNFQFASHLV LFDLPLNPDL LEQRIGRLDR
     IGQKNDIQIH LPYLEDTAQE RLMQWYHQGL NAFELTCPSG HVLYAEFAED LLNVLVGDDA
     DELTNLLNHT QSRYKELKHA MEQGRDKLLE INSHGGDRAK AIVERLAQND ENTQLIGSVI
     RLWDIIGVDQ EDKGENSIIL RPSEHMMFPT YPGLPEDGVT VTFDRDTALS RDDIALITQE
     HPLVQTGLDL ITGSETGTTS VAVLKNKALP AGTLFLELIY MADASAPKSS QLYRYLPPTP
     IRILLDKNGN DLSAKVDYAS FDKQLSAVNR HIGGKLVTAS QPILHPLFAK GEEYAQAAVD
     ELVIQAREKM TTQLTGELDR LESLKAVNPN IREEELEYLR NQMQELNTYL DASQLQLDAI
     RMVLVSHV
//
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