ID   RAPA_PECCP              Reviewed;         967 AA.
AC   C6DEY0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=PC1_3629;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001657; ACT14644.1; -; Genomic_DNA.
DR   RefSeq; WP_015841760.1; NC_012917.1.
DR   AlphaFoldDB; C6DEY0; -.
DR   SMR; C6DEY0; -.
DR   STRING; 561230.PC1_3629; -.
DR   EnsemblBacteria; ACT14644; ACT14644; PC1_3629.
DR   KEGG; pct:PC1_3629; -.
DR   eggNOG; COG0553; Bacteria.
DR   HOGENOM; CLU_011520_0_0_6; -.
DR   OMA; MSILERD; -.
DR   OrthoDB; 291634at2; -.
DR   Proteomes; UP000002736; 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..967
FT                   /note="RNA polymerase-associated protein RapA"
FT                   /id="PRO_1000216057"
FT   DOMAIN          163..333
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   DOMAIN          489..643
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   MOTIF           279..282
FT                   /note="DEAH box"
FT   BINDING         176..183
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
SQ   SEQUENCE   967 AA;  109746 MW;  77D0509AF782F50D CRC64;
     MPFTLGQRWI SDTESELGLG TVVAVDTRMI TLLFPASGEN RLYSRSDAPI TRVMFNPGDT
     VTSHEGWQLK VDDVREEKGL LVYCGQRLDD ETSAELREVF LDSKLTFNKP QDRLFAGQID
     RMDRFALRYR ARKHQNEQAL QQWGGLRGMR ASLIPHQLHI AHEVGQRHAP RVLLADEVGL
     GKTIEAGMII HQQLLAGRAS RVLIIVPETL QHQWLVEMLR RFNLLFSLFD DERYAEAKLD
     SSNPFETEQL VICSLGFVQR NAQRFAQLVN ADWDLLVVDE AHHLVWSEES PSAEYQAVET
     LARATPAVLL LTATPEQLGQ QSHFARLRLL DPNRFHDYQE FLAEQQQYRP VADAVTLLLA
     GEKAQTAELN ALSDLLGEQD IEPLLKAINS DSDDNQKARQ ELIAMLMDRH GTSRVLFRNT
     RQGVKGFPQR ILHQIRLPLP SQYQTAIKVS GIMNANKTLE VRARDMLYPE QIYQQLEGDD
     ATWWNFDPRV EWLLNYLTAN RDEKVLVICA QAATALQLEQ VLRTREAIRA AVFHEGLSIL
     ERDRAAAYFA SEEEGAQVLI CSEIGSEGRN FQFASHLVMF DLPFNPDLLE QRIGRLDRIG
     QAKEIQILVP YLENTAQAML VRWYHEGLDA FEHTCPTGRT IYDAHHAQLI ERLTTVGEQQ
     GLDEFIHTCR QQHDNLKQQL EQGRDRLLEM HSNGGEQAQL LAQAIAEQDN DVNLVTFALN
     LFDIVGINQE DRSDNLIILT PSDHMLVPDF PGLPQDGCTI TFDRDQALSR EDAQFISWEH
     PLIRNGLDLV LSGDTGSCAV SLLKNKALPV GTLLAELVYV VEAQAPKHLQ LTRFLPPTPV
     RLLMDRKGTN LAAQVEFESF NRQLNAVNRH TSSKLVNAVQ ADVHAMLQQA EALVEAQARQ
     LITEAQEQAD LQLRRELERL EALKAVNPNI REDELTALES QREQVLSNLH EANWRLDAIR
     LVVVTHQ