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 27-MAR-2024, entry version 82.
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; Pseudomonadota; 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 GeneID; 11773924; -.
DR KEGG; sbp:Sbal223_3733; -.
DR HOGENOM; CLU_011520_0_0_6; -.
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 DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd18011; DEXDc_RapA; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 2.30.30.930; -; 1.
DR Gene3D; 3.30.360.80; -; 1.
DR Gene3D; 6.10.140.1500; -; 1.
DR Gene3D; 6.10.140.2230; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 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; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR040765; Tudor_1_RapA.
DR InterPro; IPR040766; Tudor_2_RapA.
DR PANTHER; PTHR45766; DNA ANNEALING HELICASE AND ENDONUCLEASE ZRANB3 FAMILY MEMBER; 1.
DR PANTHER; PTHR45766:SF3; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A-LIKE PROTEIN 1; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 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
//
