RAPA_SHESR
ID RAPA_SHESR Reviewed; 968 AA.
AC Q0HR19;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=Shewmr7_3455;
OS Shewanella sp. (strain MR-7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60481;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-7;
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 Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. MR-7.";
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; CP000444; ABI44436.1; -; Genomic_DNA.
DR RefSeq; WP_011627271.1; NC_008322.1.
DR AlphaFoldDB; Q0HR19; -.
DR SMR; Q0HR19; -.
DR EnsemblBacteria; ABI44436; ABI44436; Shewmr7_3455.
DR KEGG; shm:Shewmr7_3455; -.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OMA; MSILERD; -.
DR OrthoDB; 291634at2; -.
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..968
FT /note="RNA polymerase-associated protein RapA"
FT /id="PRO_1000088390"
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; 109039 MW; FFE5D5F4D4CF5100 CRC64;
MPFALGQRWI SDTESELGLG TVVQVEGRMV TVLFPATGEN RMFSRNEAPL TRVIYNPGDT
VESHEGWSLS VEELTEKDGL VVYHGIHSET GEKASLRETL LNHNIRFNKP QDRLFAGQID
RLDRFGIRYQ CQLLRHQLAT SDLLGLQGPR VGLIPHQMWI AHEVGRRYAP RVLLADEVGL
GKTIEAGLII HQQLLTGRAE RVLIIVPDTL RHQWLVEMLR RFNLRFSVFD EDRCVEAFAD
HDNPFYTEQL VICSLELLRK KKRLDQALDA DWDLLVVDEA HHLEWTEEAP SRAYQVVEAL
SEVVPGVLLL TATPDQLGHE SHFARLRLLD PDRFYDYDAF LAEENSYKDV AVAAEALAGD
AKLSDAAINS LTELLSEKDI APSIRLIQAE DIDSELQQAA RSELLQELLD RHGTGRVLYR
NSRASVKGFP KRIFNAYPHA MPEQYLTAAR VNEMMGGRKT LEAKAAQALS PEKLYQEFED
NSASWWKFDP RVDWLIEFLK SHRSKKVLII ASGADTALSL EEALRTREGI QATVFHEGMS
IIERDKAGAY FAQEEGGAQA LICSEIGSEG RNFQFASHLV LFDLPLNPDL LEQRIGRLDR
IGQQNDIQIH LPYLQDTAQE RLLNWYHQGL NAFELTCPSG HVLYSEFAED LLNVLVGGDE
DELTNLLNHT QSRYKELKHA MEQGRDKLLE INSHGGDKAK AIVERLAQSD QDTKLIGSVI
RLWDIIGVDQ EDKGENSIIL RPSEHMMFPT YPGLYEDGVT VTFDRDTALS RDDIALITQE
HPLVQTGLDL ITGSDTGTTS VAILKNKALP AGTLFLELIY MADASAPKSS QLYRYLPPTP
IRVLLDKNGN DLSAKVDYTS FDKQLSAVNR HIGSKLVTAS QPILHPLFAK GEEYAQAAVN
ELVAQAREKM TSQLTGELDR LESLKAVNPN IREEELEYLR NQMQELSTYL DASQLQLDAI
RMVLVSHV
