ID   RAPA_AERS4              Reviewed;         955 AA.
AC   A4SR75;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=ASA_3426;
OS   Aeromonas salmonicida (strain A449).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=382245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A449;
RX   PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA   Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA   Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA   Brown L.L.;
RT   "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT   the evolution of a fish pathogen.";
RL   BMC Genomics 9:427-427(2008).
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; CP000644; ABO91397.1; -; Genomic_DNA.
DR   RefSeq; WP_005318987.1; NC_009348.1.
DR   AlphaFoldDB; A4SR75; -.
DR   SMR; A4SR75; -.
DR   STRING; 382245.ASA_3426; -.
DR   EnsemblBacteria; ABO91397; ABO91397; ASA_3426.
DR   KEGG; asa:ASA_3426; -.
DR   eggNOG; COG0553; Bacteria.
DR   HOGENOM; CLU_011520_0_0_6; -.
DR   OMA; MSILERD; -.
DR   OrthoDB; 291634at2; -.
DR   Proteomes; UP000000225; 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..955
FT                   /note="RNA polymerase-associated protein RapA"
FT                   /id="PRO_1000088349"
FT   DOMAIN          163..333
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   DOMAIN          478..642
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   MOTIF           279..282
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   955 AA;  107317 MW;  9609A9C95E6431F8 CRC64;
     MPFALGQRWI SDTETDLGLG TVVAVEGRMV TLLFPATGEN RMYAKEEAPV TRVSFNVGDQ
     IATHEDWTMT VEEVQEKNGL LIYVGVRTDN DEPVALKEVF LSNFIKFNKP QDRLFAGQID
     RMSRFTLRYE ALINQHKRRL NPTRGLAGGR VSLIPHQLYI AHEVGHRYAP RVLLADEVGL
     GKTIEAGMII HQQLLSGRAH RVLILLPETL QHQWLVEMLR RFNLHFSLFD EERCIEAFAD
     AENPFETEQL VICSLDFLRK KRRRFEQVLE AEWDLLVVDE AHHLEWSIDA PSRAYEMVEA
     LAEQVPGVLL LTATPDQLGH QSHFARLRLL DPERFYDYEA FLAEEQAYGK VASAAQELLD
     GETLSDEARQ ILASQLEGLD MSDAAARQQA VAKLLDQHGT GRVLFRNSRA NIQGFPERHL
     NVYPMPLPEQ YKTAIKVMGM MGGNGGDLQT RALRYLYPEK IFQQFEGENA TWTQFDPRVD
     WLLELLLSAR QQKVLVICSE AATAIALEEA LRTREGIRGT VFHEGMSILE RDKASAYFAQ
     EDGGAQVLLC SEIGSEGRNF QFASHLVLFD LPLNPDLLEQ RIGRLDRIGQ QNTVEIHVPY
     LEGTAQRALQ LWYHDGLDAF EQTCPTARPV FEAVRDELFE LLAANTGDQV TLDALLIKTR
     ELHEPLKARL EQGRDRLLEI HSSGGAAAQL LVDKLAAEDD DTGMVSFALK MFDEIGVNQD
     DRGENALVLT PGDHMLVSSF PGLPQDGMTI TFDRPTALSR DDMALLSWDH PMMRGGIDLI
     LGSEIGATSV ALLKNKALPI GSILLELIFV AESAAHPQLY RFMPPTPIRL LMDKNGQNLG
     EKVAFDAFNR QLTPVNRHLG SKLVTASQPV IHGLIGKGQV IAEELKAGIV DKARTRMAQT
     LQQDLDRLEA LKAVNPNVRD SELDYLRNLQ AELHHLIDQT QLKLDAIRFI VVTHN