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   03-AUG-2022, entry version 90.
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=ESA_03281;
OS   Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
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., Wollam A.,
RA   Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA   McClelland M., Forsythe S.J.;
RT   "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT   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 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; CP000783; ABU78503.1; -; Genomic_DNA.
DR   RefSeq; WP_012125782.1; NC_009778.1.
DR   AlphaFoldDB; A7MIC1; -.
DR   SMR; A7MIC1; -.
DR   EnsemblBacteria; ABU78503; ABU78503; ESA_03281.
DR   KEGG; esa:ESA_03281; -.
DR   PATRIC; fig|290339.8.peg.2909; -.
DR   HOGENOM; CLU_011520_0_0_6; -.
DR   OMA; MSILERD; -.
DR   OrthoDB; 291634at2; -.
DR   Proteomes; UP000000260; 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_1000088358"
FT   DOMAIN          164..334
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   DOMAIN          490..662
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;  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