ID   RAPA_SHEPA              Reviewed;         968 AA.
AC   A8H8X8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=Spea_3704;
OS   Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=398579;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700345 / ANG-SQ1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S.Z., Manno D., Hawari J., Richardson P.;
RT   "Complete sequence of Shewanella pealeana ATCC 700345.";
RL   Submitted (OCT-2007) 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; CP000851; ABV89015.1; -; Genomic_DNA.
DR   RefSeq; WP_012156899.1; NC_009901.1.
DR   AlphaFoldDB; A8H8X8; -.
DR   SMR; A8H8X8; -.
DR   STRING; 398579.Spea_3704; -.
DR   EnsemblBacteria; ABV89015; ABV89015; Spea_3704.
DR   KEGG; spl:Spea_3704; -.
DR   eggNOG; COG0553; Bacteria.
DR   HOGENOM; CLU_011520_0_0_6; -.
DR   OMA; MSILERD; -.
DR   Proteomes; UP000002608; 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_1000088385"
FT   DOMAIN          163..332
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   DOMAIN          491..678
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;  109093 MW;  25E646E65DBE1D22 CRC64;
     MPFSLGQRWI SDTESELGLG TVVGVEGRMV TVLFPATGEN RLFSRTEAPL TRVIYNPGDT
     VESHEEWKLT VTEVEEKDSL IIYHGTHSET GEQVSLRETL LNHNIRFNKP QDRLFAGQID
     RLDRFNVRYQ CQLLRNKLAT SDLLGLQGPR VGLIPHQQWI AHEVGQRFAP RVLLADEVGL
     GKTIEAGLII HQQLLTGRAE RILVIVPDTL RHQWLVEMLR RFNLRFSVFD EDRCVEAYAD
     HDNPFYTEQL VICSLDLLRK KRRLDQALDA DWDLMVVDEA HHLEWSEEAP SRAYQIVEAL
     SEEIPGVLLL TATPDQLGHQ SHFARLRLLD PDRFYDYEAF LKEEDSYKDV ATAADALASG
     EILSDESIAG LTQLLAEKDI SASITLIQDD AADADSRFQA RDELLQDLLD RHGTGRVLYR
     NSRASVKGFP VRNLHVHPQK MPEQYVTAYR VSSMMNKHLD TNAKVRQVLS PEKIYQDFDS
     GSAAWWKFDP RVDWLIDFLK NNRSKKVLII ASQAETALSL EEALRTREGI QATVFHEGMS
     IIERDKAGAY FAQESGGAQA LICSEIGSEG RNFQFASNLV LFDLPLNPDL LEQRIGRLDR
     IGQKNDVEIH LPFLANTAQE RLMQWYHQGL NAFECTCPSG HILFNEFSGE LLESLLNNDE
     AVLESLLDGT KARYQELKVA MEQGRDKLLE INSHGGERAN QLVKTLADKD EDTQLIGSVI
     RLWDIIGVEQ EDSGENAIVL HPSEHMMFPT YPGLPEDGIT VTFDREMALS RDDIALITQE
     HPLVQTGLDL ITSSETGTTS VAVLKNKALP AGTIFLELIY LADASAPKSS QLYRYLPPTP
     IRVLLDKNGN NLSDNVTYES FNKQLSAVNR HIASKLVNAS QAILHPLFAK AESFATTQLE
     TLTECAREKM TSQLSGELER LKALKAVNPN IRDEELSHLS EQMAELNRYL DSSQLQLDAI
     RLVLVSHA