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Database: UniProt
Entry: A4W6G3
LinkDB: A4W6G3
Original site: A4W6G3 
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   13-NOV-2019, entry version 83.
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=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
CC       immobilized on tightly supercoiled DNA. Does not activate
CC       transcription on linear DNA. Probably not involved in DNA repair.
CC       {ECO:0000255|HAMAP-Rule:MF_01821}.
CC   -!- SUBUNIT: Interacts with the RNAP. Has a higher affinity for the
CC       core RNAP than for the holoenzyme. Its ATPase activity is
CC       stimulated by binding to RNAP. {ECO:0000255|HAMAP-Rule:MF_01821}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RapA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01821}.
DR   EMBL; CP000653; ABP59293.1; -; Genomic_DNA.
DR   RefSeq; WP_012016015.1; NC_009436.1.
DR   STRING; 399742.Ent638_0606; -.
DR   EnsemblBacteria; ABP59293; ABP59293; Ent638_0606.
DR   KEGG; ent:Ent638_0606; -.
DR   eggNOG; ENOG4105BZK; Bacteria.
DR   eggNOG; COG0553; LUCA.
DR   HOGENOM; HOG000218482; -.
DR   KO; K03580; -.
DR   OMA; MSILERD; -.
DR   OrthoDB; 291634at2; -.
DR   Proteomes; UP000000230; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.10810; -; 2.
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_N; 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; Complete proteome; DNA-binding; Helicase;
KW   Hydrolase; Nucleotide-binding; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    968       RNA polymerase-associated protein RapA.
FT                                /FTId=PRO_1000088357.
FT   DOMAIN      164    334       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01821}.
FT   DOMAIN      490    644       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_01821}.
FT   NP_BIND     177    184       ATP. {ECO:0000255|HAMAP-Rule:MF_01821}.
FT   MOTIF       280    283       DEAH box.
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
//
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