ID   RAPA_SODGM              Reviewed;         968 AA.
AC   Q2NVX0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=SG0430;
OS   Sodalis glossinidius (strain morsitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Bruguierivoracaceae; Sodalis.
OX   NCBI_TaxID=343509;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=morsitans;
RX   PubMed=16365377; DOI=10.1101/gr.4106106;
RA   Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA   Aksoy S.;
RT   "Massive genome erosion and functional adaptations provide insights into
RT   the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL   Genome Res. 16:149-156(2006).
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; AP008232; BAE73705.1; -; Genomic_DNA.
DR   RefSeq; WP_011410293.1; NC_007712.1.
DR   AlphaFoldDB; Q2NVX0; -.
DR   SMR; Q2NVX0; -.
DR   STRING; 343509.SG0430; -.
DR   PRIDE; Q2NVX0; -.
DR   EnsemblBacteria; BAE73705; BAE73705; SG0430.
DR   KEGG; sgl:SG0430; -.
DR   eggNOG; COG0553; Bacteria.
DR   HOGENOM; CLU_011520_0_0_6; -.
DR   OMA; MSILERD; -.
DR   OrthoDB; 291634at2; -.
DR   BioCyc; SGLO343509:SGP1_RS03905-MON; -.
DR   Proteomes; UP000001932; 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_1000088396"
FT   DOMAIN          164..334
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   DOMAIN          493..644
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;  109636 MW;  17ABA88B76067EE8 CRC64;
     MPFTLGQRWI SDTENELGLG TVVAQDARMV TLLFSTSGEN RLYARTDAPI TRVMFNPGDT
     VTSHEGWQLL IDTIEEKEGL LTYIGTRLDN GETGCTLREV LLDSKLTFSK PQDRLFAGQI
     DRMDRFALRY RARKFYSEQF RAPWNGLRGI RASLIPHQLH IASEVGQRHA PRVLLADEVG
     LGKTIEAGMI IHQQMLTGRA ERVLIVVPES LLHQWLVEML RRFNLHFSLF DDERYSQSLL
     DSDNPFETEQ LVLCSLDFVR RNKERLTHLT EAEWDILVVD EAHHLAWSET APSREYQVIE
     RLAHHIPGVL LLTATPEQLG MQSHFARLRL LDPNRFHDYQ AFADEQQRYR LVADTVGLLL
     NNELLDAAAM TLLAEMLGGQ NADALLARVN EQNAADDDAR RRLTAMLMDS HGTSRVMFRN
     TRQGVKGFPA RRLHACALPL PAQYQTAFKV AGIMGGKQRL DESARHMLYP EQIFQQFEGQ
     NATWWNFDPR VQWLVDFLLD LRQEKVLVIC AHAGTALQLE QVLREREGIR AAVFHEGLSL
     VDRDRAAAYF ASAEDGAQVL LCSEIGSEGR NFQFASQMVM FDLPFNPDLL EQRIGRLDRI
     GQNRDIQIHV PYLEQSAQAV LLRWYHEGLD AFEHTCPTGR ALYDETYQTL QGYLAEPGAL
     TGLTAFIHDC RARHDALKAQ MEQGRDRLLE LHSNGGEPAR VLAQTLAEQD NDSQLVNFAL
     NLFDIIGISQ EDRSDNLLVL KPSDHMLVPD FPDVSEEGCT ITFNRDQALA REETQFISWE
     HPIIRNGLDL VLSSESGNSA LSLLKNKALP VGTLLLELIY VVESQAPRNL QLNRFLPATP
     LRLLLDKNGT NLAPQVEFEQ FNRQLNAVKR HTASKLVSAV QPEVHGMLTH GEHLVAEQAQ
     ALIDEARAQA DLLLSAELSR LKALRAVNPA IRDNELEAVA ENRRQVLRHL DEASWRLDAI
     RLIVVTHQ