ID   RAPA_ERWT9              Reviewed;         968 AA.
AC   B2VGQ6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=ETA_07300;
OS   Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS   4357 / Et1/99).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=465817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99;
RX   PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA   Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA   Geider K.;
RT   "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT   bacterium in the genus Erwinia.";
RL   Environ. Microbiol. 10:2211-2222(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; CU468135; CAO95776.1; -; Genomic_DNA.
DR   RefSeq; WP_012440478.1; NC_010694.1.
DR   AlphaFoldDB; B2VGQ6; -.
DR   SMR; B2VGQ6; -.
DR   STRING; 465817.ETA_07300; -.
DR   EnsemblBacteria; CAO95776; CAO95776; ETA_07300.
DR   KEGG; eta:ETA_07300; -.
DR   eggNOG; COG0553; Bacteria.
DR   HOGENOM; CLU_011520_0_0_6; -.
DR   OMA; MSILERD; -.
DR   OrthoDB; 291634at2; -.
DR   Proteomes; UP000001726; 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; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..968
FT                   /note="RNA polymerase-associated protein RapA"
FT                   /id="PRO_1000188177"
FT   DOMAIN          164..334
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   DOMAIN          490..643
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;  109531 MW;  280262A1A6F16FA1 CRC64;
     MPFTLGQRWI SDTESELGLG TVVAVDTRMV TLLFPATGEN RLYARNDSPI TRVVFNPGDT
     ITSHEGWQLD VDEITTANGV VSYIGTRLDT SETGVVLREV MLDSKLVFGK PQDRLFAGQL
     DRMDRFALRF RARKYQSEQY RLATSGLRGM RTSLIPHQLH IAHDVGRRHA PRVLLADEVG
     LGKTIEAGMI IHQQLQAGRA ERVLIVVPET LQHQWLVEML RRFNLRFALF DDDRYAQAQL
     DSDNPFDTEQ MIICSLDFVR RNKQRLEKLA DAEWDLMVVD EAHHLVWSED APSREYQVIE
     QLAEQVPGIL LLTATPEQLG MESHFARLRL LDPDRFHDFA QFVEEQKHFS PIADAVTLLL
     ADQKIGNDEL NLLNDLMGEQ DIEPLLQTAN SDREGKLAAR QELISMLMDR HGTSRVLFRN
     TRNGVKGFPK RELHQIRLPL PTQYQTAIKV SGIMSARKTA DERAQDMLYP EQIYQEFEGD
     SGTWWNFDPR VEWLMGYLTS NRDKKVLVIC AKAATALQLE QVLREREGIR AAVFHEGLSI
     IERDRAAAWF ASEEDGAQVL LCSEIGSEGR NFQFASQMVM FDLPFNPDLL EQRIGRLDRI
     GQVHDIQIHV PYLEKTAQAV LVQWYHEGLD AFEHTCPTGR AVYDSVYTQL IAYLAAPENS
     EGLEAFIQHC RKQHDTLKAQ LEQGRDRLLE LNSNGGEKGQ ALADMIAEQD NNIELVNFAL
     NLFDIVGINQ EDRSDNLIVL TPGDHMLVPD FPGLPEDGCT ITFDRNQALS REDAQYVSWE
     HPIIRNGLDL ILSGDTGSCA ISLLKNKALP VGTLLVELIY VVEAQAPKHL QLTRFLPPTP
     IRMMVDRKGN NLAAKVEFES FNRQLNAVNR HTGSKLVNAV QSDVHEIITL SEDQAAAEAR
     KVIDAARQEA DEKLSAELSR LQALSAVNPN IRQDEIDALE SNRQQVLSNL DEAGWRLDAL
     RLIVVTHQ