RAPA_PHOLL
ID RAPA_PHOLL Reviewed; 970 AA.
AC Q7N8V1;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
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}; Synonyms=hepA;
GN OrderedLocusNames=plu0615;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
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; BX571861; CAE12910.1; -; Genomic_DNA.
DR RefSeq; WP_011144992.1; NC_005126.1.
DR AlphaFoldDB; Q7N8V1; -.
DR SMR; Q7N8V1; -.
DR STRING; 243265.plu0615; -.
DR PRIDE; Q7N8V1; -.
DR EnsemblBacteria; CAE12910; CAE12910; plu0615.
DR GeneID; 24168038; -.
DR KEGG; plu:plu0615; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OMA; MSILERD; -.
DR OrthoDB; 291634at2; -.
DR BioCyc; PLUM243265:PLU_RS03030-MON; -.
DR Proteomes; UP000002514; 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..970
FT /note="RNA polymerase-associated protein RapA"
FT /id="PRO_0000207179"
FT DOMAIN 164..334
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT DOMAIN 490..663
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 970 AA; 111060 MW; 9D9FF7622B67FB71 CRC64;
MPFTLGQRWI SDTESELGLG TVVALDARMV TLLFPASGEN RLYARNDSPI TRVMFNSGDV
VTSHEGWQLK VDEIQQENGL LIYTGTRLDT LEENISLREV FLDSKLTFNK PQDRLFAGQI
DRMDRFALRF RARKYQSEQF KLAESGLRGI RASLIPHQLH IANEVGKRYA PRVLLADEVG
LGKTIEAGMI IHQQLLAGRA ERVLVIVPDS LQHQWLVEML RRFNLRFALF DDSRYIEARH
DSDNPFETEQ LVLCSLDFAR RNKQRFEHML EASWDLMVVD EAHHLVWSED APSREYQVVE
QLAEQIPSVL LLTATPEQLG QESHFARLRL LDPNRFHDYQ TFIDEQQKYR PVADAVTLLL
SGEQLNNNQL NLMGELISEQ NIEPLLKAAN SNSGESETAR RELISMLMDR HGTSRILFRN
TRNGVKGFPH RELHQIKLPL PSQYQTAIKV SDIMGAKKSL EARAWDMLYP EQIYQEFEGE
NATWWNFDPR VEWLLGFLMA NRHEKVLVIC AKATTALQLE QVLREREGIR GAVFHEGLSL
IERDRAAAYF ASEEEGAQVL LCSEIGSEGR NFQFANQLVM FDLPFNPDLL EQRIGRLDRI
GQSRDIQISV PYLENTAQAV LIRWYHEGLD AFEHTCPTGR TIYDHYYEAL LNYLAKPNNQ
DQEKFGEFID QCRQQHEQLK QQLEQGRDRL LEMNSNGGEH GLRLAEKISE YDNDTELVNF
SLNLFDIVGI NQEDRNDNMI VLTPSDHMLV PDFPGLPKDG CTITFDREQS LSREDAQFIS
WEHPIIRNGL DLILSGDTGS CAVSLLKNKA LPVGTLLVEL IYVVEAQAPK RLQLTRFLPP
TPLRILMDLK GNNLADQVEF ESFNRQLNAV NRHTASKLVN AVQKEVHAIL QQAEGLVETQ
AKSLIEQAEQ EADENLAAEL SRLEALKTVN PNIRDDELEA IEANRQQLLL NLNQASWRLD
AIRLVVVTHQ
