ID   RAPA_ENT38              Reviewed;         968 AA.
AC   A4W6G3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=Ent638_0606;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638;
RX   PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA   Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA   Vangronsveld J., Newman L., Monchy S.;
RT   "Genome sequence of the plant growth promoting endophytic bacterium
RT   Enterobacter sp. 638.";
RL   PLoS Genet. 6:E1000943-E1000943(2010).
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; CP000653; ABP59293.1; -; Genomic_DNA.
DR   RefSeq; WP_012016015.1; NC_009436.1.
DR   AlphaFoldDB; A4W6G3; -.
DR   SMR; A4W6G3; -.
DR   STRING; 399742.Ent638_0606; -.
DR   EnsemblBacteria; ABP59293; ABP59293; Ent638_0606.
DR   KEGG; ent:Ent638_0606; -.
DR   eggNOG; COG0553; Bacteria.
DR   HOGENOM; CLU_011520_0_0_6; -.
DR   OMA; MSILERD; -.
DR   OrthoDB; 291634at2; -.
DR   Proteomes; UP000000230; 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_1000088357"
FT   DOMAIN          164..334
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   DOMAIN          490..644
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   MOTIF           280..283
FT                   /note="DEAH box"
FT   BINDING         177..184
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
SQ   SEQUENCE   968 AA;  109742 MW;  3E0FECDECF16A11D CRC64;
     MPFTLGQRWI SDTESELGLG TVVALDARMV TIMFPATGEN RLYARNDSPV TRVMFNPGDT
     VTSHEGWQLK IEDVKEENGL LAYTGTRLDT DEADVMLREV MLDSRLVFSK PQDRLFAGQI
     DRMDRFSLRY RARKFQSEQY RMPWSGLRGQ RTSLIPHQLN IAHDVGRRHA PRVLLADEVG
     LGKTIEAGMI LHQQLLSGAA ERVLIVVPET LQHQWLVEML RRFNLRFSLF DDERYAEAQH
     DADNPFETEQ LVICSLDFVR RSKQRLEHLC DAEWDLLVVD EAHHLVWSEN APSREYMAIE
     QLAERVPGIL LLTATPEQLG LESHFARLRL LDPNRFHDFD VFVEEQQNYR PVADAVAMLL
     AGKHLSNDEL NTLSDLIGEQ DIEPLLHTAN SDRDGADAAR QELVSMLMDR HGTSRVLFRN
     TRNGVKGFPK RELHTIKLPL PTQYQTAIKV SGIMGARKSA EERARDMLYP EQIYQEFEGD
     TGTWWNFDPR VEWLMGYLTA HRSQKVLVIC AKAATALQLE QVLREREGIR AAVFHEGMSI
     IERDRAAAWF GEEDSGAQVL LCSEIGSEGR NFQFASKLVM FDLPFNPDLL EQRIGRLDRI
     GQAHDIQIHV PYLENTAQSV LVRWFHEGLD AFEHTCPTGR TIYDQVHSDL IGYLASPENT
     DGFDDLIKTC REKHDALKIQ LEQGRDRLLE IHSNGGEKAQ ALAESIEEQD DDTSLISFAM
     NLFDIVGINQ DDRGENMIVL TPSDHMLVPD FPGLPEDGCT ITFERDVALS REDAQFITWE
     HPLIRNGLDL ILSGDTGSST ISLLKNKALP VGTLLLELIY VVEAQAPKQL QLNRFLPATP
     VRLMLDKNGT NLAAQVEFES FNRQLSAVNR HTGSKLVNAV QQDVHAILQQ GEAQIEKAAR
     ALIDSARREA DEKLSAELSR LEALRAVNPN IRDDELAAIE SNRQQVLESL DQASWRLDAL
     RLIVVTHQ