RAPA_PHOPR
ID RAPA_PHOPR Reviewed; 972 AA.
AC Q6LV34;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=PBPRA0409;
OS Photobacterium profundum (strain SS9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9;
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
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; CR378664; CAG18841.1; -; Genomic_DNA.
DR RefSeq; WP_011217198.1; NC_006370.1.
DR AlphaFoldDB; Q6LV34; -.
DR SMR; Q6LV34; -.
DR STRING; 298386.PBPRA0409; -.
DR PRIDE; Q6LV34; -.
DR EnsemblBacteria; CAG18841; CAG18841; PBPRA0409.
DR KEGG; ppr:PBPRA0409; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OMA; MSILERD; -.
DR OrthoDB; 291634at2; -.
DR Proteomes; UP000000593; Chromosome 1.
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..972
FT /note="RNA polymerase-associated protein RapA"
FT /id="PRO_0000207180"
FT DOMAIN 164..334
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT DOMAIN 493..671
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 972 AA; 109810 MW; 12F32F82583B5DDB CRC64;
MPFTLGQRWI SDTESDLGLG TVVAEDKRTV SIMFSACEES RLYARSDAPV TRVMFNVGDV
VESHEGWSLE VKIVEENGGI FTYIGTRTDT EEENVKLREI FLSHQIRFNK PQDKLFAGQI
DRMDRFALRY RALTNQYEQH KSPLRGLCGM RAGLIPHQLF IAHEVGRRYA PRVLLADEVG
LGKTIEAGMI IHQQVLAGRA ERILIVVPET LQHQWLVEMM RRFNLHFSIF DEERCVESLA
DATNPFETAQ YVLCSLDFLR KSRRRFEQAQ DADWDLLVVD EAHHLEWSED KPSRQYQVVE
ALAEATPGVL LLTATPEQLG RESHFARLRL LDPDRFYDYD TFVEEERQYA PVAEAVTRLL
SGEKIDDNAR KTLVDLLSEQ DIEPKLRLIE SSDADDEHAQ TVRHELIDSL MDRHGTGRVL
FRNTRAAIKG FPERHLNMYP LELPSQYKTA MRVSSMMSGS ISAEQKAIKL LYPEDIYQEF
EGESATWWNF DPRVNWLLEM LKANRNEKVL VICSRAQTAL TLEQALRERE GIRATVFHEG
MSIIDRDKAA AYFAQEDDGA QVLLCSEIGS EGRNFQFSNQ LVMFDLPNNP DLLEQRIGRL
DRIGQQRDIE IHVPHLEGTS QALLAHWYNE GLNSFEETCP TGRAVYEAVS DDLIALLACE
KHEPEALENL IEKSAAMHHE LKAKLDQGRD RLLEIHSNGG NAANDLVTQI SSKDGDTNLI
AFSLGLFDTI GLNQDDKGEN AIVVTPSEHM MVASYPGLPY DGCTITFDRE TALSREDLHF
ISWEHPMIQG GIDLLLSEGV GATAVSLLKN KALPAGTLLL EMVYVVDAQA PKSSGIGRFL
PKTPIRILLD AKGNNLSNKV AFEGFNRQLS PVNRHLASKL VNSVQKEIHV LIAQAEQEVA
KELVTVRESA QTEMENSLQA ELTRLQALKA VNPNIRDDEL ELIESQIQDL TGYIGKAQIQ
LDSLRLIVVS HN
