ID   RAPA_SERP5              Reviewed;         968 AA.
AC   A8G9P6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=Spro_0730;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-2007) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000826; ABV39836.1; -; Genomic_DNA.
DR   RefSeq; WP_012005181.1; NC_009832.1.
DR   AlphaFoldDB; A8G9P6; -.
DR   SMR; A8G9P6; -.
DR   STRING; 399741.Spro_0730; -.
DR   EnsemblBacteria; ABV39836; ABV39836; Spro_0730.
DR   KEGG; spe:Spro_0730; -.
DR   eggNOG; COG0553; Bacteria.
DR   HOGENOM; CLU_011520_0_0_6; -.
DR   OMA; MSILERD; -.
DR   OrthoDB; 291634at2; -.
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_1000088376"
FT   DOMAIN          164..334
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   DOMAIN          490..664
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;  110102 MW;  C7852DA848FD6873 CRC64;
     MPFTLGQRWI SDTESELGLG TVVALDTRMI TLLFPATGEN RLYARNDSPI TRVMFNPGDT
     ISNHEGWELQ VEEVKEENGL LTYIGTRLDT QESGVAMREV LLDSKLTFSK PQDRLFAGQI
     DRMDRFALRF RARKYQSEQY RLPFAGLRGM RASLIPHQLH IAYEVGQRHA PRVLLADEVG
     LGKTIEAGMI IHQQLLAGRA ERVLIVVPET LQHQWLVEMM RRFNLYFSLF DDSRYSEAKL
     DSSNPFETEQ LVICSLDFVR RNKLRLEELA DAQWDLLVVD EAHHLAWSEE APSREYQVIE
     QLAEHIPGVL LLTATPEQLG QQSHFARLRL LDPNRFHDYQ DFVAEQQKYR PVADAVTLLL
     SGERLADDKL NLLGELIDEQ DIEPLLKAAN SDSDNSEQAR QELVTMLMDR HGTSRVLFRN
     TRNGVKGFPH RFLHQIKLPL PTQYQTAIKV SGIMGAKKTV EARARDMLYP EQIYQEFEGE
     NATWWNFDPR VEWLLNYLVA NRHEKVLVIC AHAATALQLE QVLREREAIR AAVFHEGLSI
     IERDRAAAYF ASEEDGAQVL LCSEIGSEGR NFQFASHLVM FDLPFNPDLL EQRIGRLDRI
     GQMHDIQIMV PYLENTAQAV LGRWFHEGLD AFEHTCPTGR TIYDSGYEQL IGFLAAPTEQ
     EGLDEFIHHC RQQHDHLKVQ LEQGRDRLLE MHSNGGEKAQ ALAEAIANQD NDVNLVGFAL
     NLFDIVGINQ DDRSDNLIVL TPSDHMLVPD FPGLPQDGCT VTFDREQALS REDAQFVSWE
     HPIIRNGLDL ILSGDTGSCA VSLLKNKALP VGTLLVELVY VVEAQAPKHL QLTRFLPPTP
     IRMLMDRKGT NLAAQVEFES FNRQLNAVNR HTSSKLVNAV QQDVHAMLQQ AESLVEEQAR
     ALIEQAKQEA DDKLSTELAR LEALKAVNPN IRDDEVEALE FNRKQVLVNL NEAGWRLDAI
     RLVVVTHQ