ID   RAPA_PROMH              Reviewed;         967 AA.
AC   B4F2H6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, 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}; OrderedLocusNames=PMI2328;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320;
RX   PubMed=18375554; DOI=10.1128/jb.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.T.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(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; AM942759; CAR44604.1; -; Genomic_DNA.
DR   RefSeq; WP_004249485.1; NC_010554.1.
DR   AlphaFoldDB; B4F2H6; -.
DR   SMR; B4F2H6; -.
DR   STRING; 529507.PMI2328; -.
DR   EnsemblBacteria; CAR44604; CAR44604; PMI2328.
DR   GeneID; 6801169; -.
DR   KEGG; pmr:PMI2328; -.
DR   eggNOG; COG0553; Bacteria.
DR   HOGENOM; CLU_011520_0_0_6; -.
DR   OMA; MSILERD; -.
DR   Proteomes; UP000008319; 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..967
FT                   /note="RNA polymerase-associated protein RapA"
FT                   /id="PRO_1000188180"
FT   DOMAIN          163..333
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   DOMAIN          489..660
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;  110486 MW;  75FBF33023B316DE CRC64;
     MPFTLGQRWI SDTESELGLG TVVAIDARMV TLLFPACGEN RLYSRHDAPI TRVMFNVGDT
     VTSHEGWKLA IDNVVEDNGL LIYHGVRLDT EEPAQLREVF LDNKLTFNKP QDRLFAGQID
     RMDRFALRYR ARKFMSEQFK QAQSGLRGIR ASLIPHQLYI ANEVGKRHNP RVLLADEVGL
     GKTIEAGMII HQQIMDGRAE RVLIIVPESL QHQWLVEMLR RFNLRFSLFD DSRYSESLLD
     SDNPFETEQM IICSLDFVRK NKQRFEHLVE ATWDMLVVDE AHHLVWSEKA PSREYQVIET
     LAEAIPSVLL LTATPEQLGQ ESHFARLRLL DPNRFHDYNE FINEQQKYRP VADAVTILLS
     EDDLNNEQQN SISEMISEQD IEPLLKASNT QGEERTKSRQ ALIHMLMDRH GTGRLLFRNT
     RSGVKGFPNR LLHAIKMPLP TQYQTAIKVA EIMAAKKSLE VRAKEMLYPE RIYQEFEGEN
     ATWWNFDPRV EWLLGFLTAN RHEKVLVICA QAATALQLEQ VLREREGIRA AVFHEGMSLL
     ERDRAAAYFA SEEEGAQVLL CSEIGSEGRN FQFANQLVMF DLPFNPDLLE QRIGRLDRIG
     QNRDIDISVP YLEGTAQSVL LRWYHEGLDA FEHTCPTGRT IYDNEYDALV NYLAQPNELG
     DFDKFIVSCR KQHDEMKLKL EQGRDRLLEM HSNGGEVGVE LANKIAEQDN DPDLVNFALN
     LFDIVGINQE DRSDSLIVLT PSDHMLVPDF PGLPQDGCTI TFDREHALSR EDTQFISWEH
     PIIRNGLDLV LSGDTGSCAV SLLKNKALPV GTLLVELIYV VEAQAPKHLH LTRFLPATPV
     RLLLDLKGNN LASQVEFESF NRQLNAVNRH TSSKLVNAVQ NEVHHVLKAS ESLMEAEAKT
     LIEQAKQEAD NALTHELSRL EALRAVNPNI RDDEVEAIEN ERTHILNHLD EATWRLDAIR
     LIVVTHQ