RAPA_SHEFN
ID RAPA_SHEFN Reviewed; 968 AA.
AC Q07XC8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=Sfri_3508;
OS Shewanella frigidimarina (strain NCIMB 400).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318167;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 400;
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., Pitluck S.,
RA Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL Submitted (AUG-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 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; CP000447; ABI73336.1; -; Genomic_DNA.
DR RefSeq; WP_011638927.1; NC_008345.1.
DR AlphaFoldDB; Q07XC8; -.
DR SMR; Q07XC8; -.
DR STRING; 318167.Sfri_3508; -.
DR EnsemblBacteria; ABI73336; ABI73336; Sfri_3508.
DR KEGG; sfr:Sfri_3508; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OMA; MSILERD; -.
DR OrthoDB; 291634at2; -.
DR Proteomes; UP000000684; 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_1000088382"
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; 109766 MW; 6D45FF3ED5267770 CRC64;
MPFALGQRWI SDTESELGLG TVVQVEGRMV TLLFPATGEN RMFSRSEAPL TRVIFNPGDT
VESGEGWSIT IEELEEKNQL VIYHGIHSET QEKVSLRETM LSHNIRFNKP QDRLFAGQID
RLERFGVRYQ CQLLRHKLAT SDLLGQQGPR VGLIAHQQWI AHEVGSRYAP RVLLADEVGL
GKTIEAGLII HQQLLTGRAE RILVIVPDTL RHQWLVEMLR RFNLRFSVFD EDRCVEAYAD
NDNPFYTEQL IICSLDLLRK KKRLEQAVDA DWDLMVVDEA HHLEWSEDAP SRAYKIVEAL
SEVVPGVLLL TATPDQLGHQ SHFARLRLLD PDRFYDYDAF LAEEASYKDV AEAAEALSQD
KKLPDSAINS LTELLSEKDI EPSIRLIQSK DVDAESQQAA RQELLQELLD RHGTGRVLYR
NSRASVKGFP KRLFNAYPHD MPAQYVTAER VNAMMGSAKQ PQAKAAQALS PEKLYQAFEN
DSASWWKFDP RVDWLIEFLK SHRSKKVLII ASQAETALSL EEALRTREGI QATVFHEDMS
IIERDKAGAY FAQEEGGAQA LICSEIGSEG RNFQFASHLI LFDLPLNPDL LEQRIGRLDR
IGQQNDIQIH LPYLRDTAQE RLMRWYHQGL NAFELTCPSG HVLFNEFADE LINVLCDDDE
DLMTQLLNHT QHRYKELKQA MEQGRDKLLE INSHGGERAN ALIKRLSDSD NDTHLIGSVI
RLWDIIGVDQ EDRGENSIIL RPSEHMMFPT YPGLNEDGIT VTFDRETALS RDDIAFITQE
HPLVQTGLDL ITGSETGTTS VAILKNKALP AGTLFLELIY MADASAPKST QLYRYLPPTP
IRVLLDKNGL NMADKVDYAS FDKQLSAVNR HIASKLVNAS QPILHPLLAK GEEYAKESLT
QLVVDARAKM TQQLTGELER LEALKAVNPN IREDELEYIR NQMTEITGYM DNSQLQLDAI
RMVLVSHV
