ID   RAPA_SHEB2              Reviewed;         968 AA.
AC   B8ECC6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=Sbal223_3733;
OS   Shewanella baltica (strain OS223).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=407976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS223;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ovchinnikova G., Brettar I., Rodrigues J., Konstantinidis K.,
RA   Tiedje J.;
RT   "Complete sequence of chromosome of Shewanella baltica OS223.";
RL   Submitted (DEC-2008) 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; CP001252; ACK48211.1; -; Genomic_DNA.
DR   RefSeq; WP_012197673.1; NC_011663.1.
DR   AlphaFoldDB; B8ECC6; -.
DR   SMR; B8ECC6; -.
DR   EnsemblBacteria; ACK48211; ACK48211; Sbal223_3733.
DR   GeneID; 11773924; -.
DR   KEGG; sbp:Sbal223_3733; -.
DR   HOGENOM; CLU_011520_0_0_6; -.
DR   OMA; MSILERD; -.
DR   Proteomes; UP000002507; 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; Transcription; Transcription regulation.
FT   CHAIN           1..968
FT                   /note="RNA polymerase-associated protein RapA"
FT                   /id="PRO_1000188190"
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;  108986 MW;  779C13E1A0E2DDAA CRC64;
     MPFALGQRWI SDTESELGLG TVVQVEGRMV TVLFPATGEN RMFSRAEAPL TRVIYNPGDS
     VESHEGWSLA VSELTEKDGI VIYHGIHSET GEQVTLRETL LNHNIRFNKP QDRLFAGQID
     RLDRFGVRYQ CQMLRHKLAS SDLLGLQGPR VGLIPHQMWI AHEVGRRYAP RVLLADEVGL
     GKTIEAGLII HQQLLTGRAE RILIIVPDTL RHQWLVEMLR RFNLRFSVFD EDRCVEAYAD
     HDNPFYTEQL VICSLELLRK KKRLDQALDA DWDLLVVDEA HHLEWTEEAP SRAYQVVEAL
     SEVIPGVLLL TATPDQLGHE SHFARLRLLD PDRFYDYDAF LAEEDSYKDV AIAAEALAGN
     AKLPDAAINS LTELLGEKDI SPSIRLIQAD GIDAEVQQAA RSELLQELLD RHGTGRVLYR
     NSRASVKGFP KRFFNAYPHA MPDQYQTAAR VSGMMGGHKS LEAKAAQALS PEKLYQEFED
     NSASWWKFDP RVDWLIEFLK SHRSKKVLII ASQAETALSL EEALRTREGI QATVFHEGMS
     IIERDKAGAY FAQEEGGAQA LICSEIGSEG RNFQFASHLV LFDLPLNPDL LEQRIGRLDR
     IGQKNDIQIH LPYLEDTAQE RLMQWYHQGL NAFELTCPSG HVLYSEFAED LLNVLVVDDS
     DELTNLLNHT QSRYKELKHA MEQGRDKLLE INSHGGEKAM AIVQRLAQND GDTHLIGSVI
     RLWDIIGVDQ EDKGENSIIL RPSEHMMFPT YPGLPEDGVT VTFDRDTALS RDDIALITQE
     HPLVQTGLDL ITGSETGTTS VAILKNKALP AGTLFLELIY MADASAPKSS QLYRYLPPTP
     IRVLLDKNGN DLSAKVDYAS FDKQLSAVNR HIGGKLVTAS QPILHPLFAK GEEYAQVVVD
     EMVAQAREKM TQQLSAELSR LESLKAVNPN IREEELEYLR NQMQELNTYL DASQLQLDAI
     RMVLVSHV