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Database: UniProt
Entry: A7MIC1
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Original site: A7MIC1 
ID   RAPA_CROS8              Reviewed;         968 AA.
AC   A7MIC1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   19-FEB-2014, entry version 44.
DE   RecName: Full=RNA polymerase-associated protein RapA;
DE            EC=3.6.4.-;
DE   AltName: Full=ATP-dependent helicase HepA;
GN   Name=rapA; OrderedLocusNames=ESA_03281;
OS   Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-894;
RX   PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA   Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA   Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D.,
RA   Wollam A., Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K.,
RA   Wilson R.K., McClelland M., Forsythe S.J.;
RT   "Genome sequence of Cronobacter sakazakii BAA-894 and comparative
RT   genomic hybridization analysis with other Cronobacter species.";
RL   PLoS ONE 5:E9556-E9556(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       (By similarity).
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 (By similarity).
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RapA
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
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DR   EMBL; CP000783; ABU78503.1; -; Genomic_DNA.
DR   RefSeq; YP_001439339.1; NC_009778.1.
DR   ProteinModelPortal; A7MIC1; -.
DR   STRING; 290339.ESA_03281; -.
DR   EnsemblBacteria; ABU78503; ABU78503; ESA_03281.
DR   GeneID; 5551528; -.
DR   KEGG; esa:ESA_03281; -.
DR   PATRIC; 20398290; VBICroSak107175_2909.
DR   eggNOG; COG0553; -.
DR   HOGENOM; HOG000218482; -.
DR   KO; K03580; -.
DR   OMA; WDLMVVD; -.
DR   OrthoDB; EOG6D2KQT; -.
DR   ProtClustDB; PRK04914; -.
DR   BioCyc; CSAK290339:GJ80-3271-MONOMER; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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; IPR000330; SNF2_N.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF12137; RapA_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 3.
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; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    968       RNA polymerase-associated protein RapA.
FT                                /FTId=PRO_1000088358.
FT   DOMAIN      164    334       Helicase ATP-binding.
FT   DOMAIN      490    662       Helicase C-terminal.
FT   NP_BIND     177    184       ATP (By similarity).
FT   MOTIF       280    283       DEAH box.
SQ   SEQUENCE   968 AA;  109784 MW;  D1455F50E48804DB CRC64;
     MPFTLGQRWI SDTESELGLG TVVAIDARMV TLLFPATGEN RLYARNDSPV TRVMFNPGDT
     VTSHEGWQLK VDEVKEENGL LIYIGTRLDT LEENVALREV FLDSKLVFSK PQDRLFAGQI
     DRMDRFALRY RARKYQSEQY RMPWSGLRGQ RTNLIPHQLN IANDVGRRHA PRVLLADEVG
     LGKTIEAGMI IHQQLLAGAA ERVLIVVPET LQHQWLVEML RRFNLRFSLF DDERYAEAQH
     ESDNPFDTEQ LVICSLDFVR RNKQRLEHLC DAEWDLLVVD EAHHLVWSED APSREYQAIE
     QLAERVPGVL LLTATPEQLG MESHFARLRL LDPNRFHDFA QFVEEQQNYR PVADAVALLL
     AGTHLSDEQL NTLSELIGEQ DIEPLLQTAN SDRDGAESAR QELVSMLMDR HGTSRVLFRN
     TRNGVKGFPQ RELHTIKLPL PTQYQTAIKV SGIMGARKSA EERARDMLYP EQIYQEFEGD
     SGTWWNFDPR VEWLMGYLTS HRSQKVLVIC AKAATALQLE QVLREREGIR AAVFHEGMSI
     IERDRAAAWF AEEDTGAQVL LCSEIGSEGR NFQFASQLVM FDLPFNPDLL EQRIGRLDRI
     GQAHDIQIHV PYLEKTAQSV LVRWYHEGLD AFEHTCPTGR AIYDSVYEQL IGYLAAPENT
     EGFDALIQAC RKQHDELKAQ LEQGRDRLLE IHSNGGEKAQ QLADAIAEQD DDTGLVNFAM
     NLFDIVGINQ DDRGEHMIVL TPSDHMLVPD FPGLPEDGCT ITFNRDVALS REDAQFITWE
     HPLIRNGLDL ILSGDTGSCT ISLLKNKALP VGTLLLELIY VVEAKAPKQL QLNRFLPPTP
     VRMLLDKNGN NLAGQVEFES FNRQLSAVNR HTGSKLVNAV QQEVHAILQG GEAQVEKAAR
     ELIDAARQEA DDKLSAELSR LEALRAVNPN IRDDELAAIE HNRQQVLENL NQASWRLDAL
     RLIVVTHQ
//
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