RAPA_ACTP2
ID RAPA_ACTP2 Reviewed; 969 AA.
AC A3MZ32;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=APL_0314;
OS Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=416269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L20;
RX PubMed=18065534; DOI=10.1128/jb.01845-07;
RA Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA Nash J.H.E.;
RT "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT (serotype 5b).";
RL J. Bacteriol. 190:1495-1496(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; CP000569; ABN73418.1; -; Genomic_DNA.
DR RefSeq; WP_009874664.1; NC_009053.1.
DR AlphaFoldDB; A3MZ32; -.
DR SMR; A3MZ32; -.
DR STRING; 416269.APL_0314; -.
DR PRIDE; A3MZ32; -.
DR EnsemblBacteria; ABN73418; ABN73418; APL_0314.
DR KEGG; apl:APL_0314; -.
DR PATRIC; fig|416269.6.peg.322; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OMA; MSILERD; -.
DR Proteomes; UP000001432; 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..969
FT /note="RNA polymerase-associated protein RapA"
FT /id="PRO_1000088346"
FT DOMAIN 162..339
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT DOMAIN 492..663
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT MOTIF 285..288
FT /note="DEAH box"
FT BINDING 175..182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
SQ SEQUENCE 969 AA; 109747 MW; 1AC53AB2951DA0E0 CRC64;
MFVVGQRWIS ESENNLGLGI VTASDNRTVT IQFPAAEEER IYALSVAPLT RVQFQKGDRI
NSVEGWQLDV EEVVENQGFI IYLGKRADSG EEAVLPEMQL DHKVSFSKPQ DRLFSAQIDR
SDRFALRYRA LQHQQAQFQS PLRGMRGIRA SLIPHQLHIA KEVGQRVAPR VLLADEVGLG
KTIEAGMILQ QQLFSGRVER VLVLVPESLQ HQWLVEMLRR FNLKFSLFDE ERCSDFDKAD
EDGNDVSENP FDSEALVIAS IDWLESSPNR AKQVLASHWD MLIVDEAHHL AWSENEPSVG
YQFVERLSKQ TPAVLLLTAT PEQLGQESHF ARLALLDADR FYDYHSFIAE QKDYKPVADA
VATLLNDKPL SHDEQNSIAE LLSEKDTEPM FKVINSEKSK ENDRLQVRQE LIRELIDRHG
TSRVLFRNTR QGVKGFPHRV YHQITLEMPS QYTNALKVMG MMGGVTKDDQ LYPERLFQRM
NPAAKWADFD PRIEWLITFL KNHRDEKILV ICKQADTAIA LEQILREREA IRSAVFHEKM
SIVERDRASA YFAQMEEGAQ VLISSSIGSE GRNFQFASNL VLFNLPDNPD LLEQSIGRLD
RIGQKNDIQI HVPCFENSMQ MVLATWYHQG LNAFEETCPM GAALFREFGE ELEGFLKNPQ
AVGFDEFLVR TFKRQQQLKA ELEQGRDRLL ELNSNGGEVA QALAEAIAKE DNNPHLVNFA
LSLFDVIGLE QEDLGEQSIV ISPTGHMLVP DFPGIAEDST TVTFDRQLAL MREDVEFLTW
DHPMIRNGID LITSGDIGKS AISLLINKHL PAGTLLLEAI YMVETQAPKG LNLTRFLPPT
PVRILLGNKG NDMAAQVSFT GLEKQLKPVN KQMANKIAKM AQADIKKLID ISEQKIAAKL
PELIEKASQD ADSTLSAELY RLTSLQAVNK NIRADEIEAL EQQRIESLKQ IALANWRLDS
LRVIVSNKE