RAPA_ACTSZ
ID RAPA_ACTSZ Reviewed; 966 AA.
AC A6VQU2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=Asuc_1992;
OS Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS 130Z).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=339671;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z;
RX PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA Burkhart K.B., Harkins V., Vieille C.;
RT "A genomic perspective on the potential of Actinobacillus succinogenes for
RT industrial succinate production.";
RL BMC Genomics 11:680-680(2010).
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; CP000746; ABR75339.1; -; Genomic_DNA.
DR RefSeq; WP_012073716.1; NC_009655.1.
DR AlphaFoldDB; A6VQU2; -.
DR SMR; A6VQU2; -.
DR STRING; 339671.Asuc_1992; -.
DR PRIDE; A6VQU2; -.
DR EnsemblBacteria; ABR75339; ABR75339; Asuc_1992.
DR KEGG; asu:Asuc_1992; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OMA; MSILERD; -.
DR OrthoDB; 291634at2; -.
DR Proteomes; UP000001114; 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..966
FT /note="RNA polymerase-associated protein RapA"
FT /id="PRO_1000088347"
FT DOMAIN 163..337
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT DOMAIN 488..642
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT MOTIF 283..286
FT /note="DEAH box"
FT BINDING 176..183
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
SQ SEQUENCE 966 AA; 110092 MW; A3F840BB90ABAD77 CRC64;
MVFAVGQRWI SESENNLGLG IITEVNSRAV TIFFPAADET RIYATASAPL TRVVFNAGDM
ITHQQGWQAQ VTDIMVNNLT ALYLVRRTDN GEEIVLKEID LAHQINFSQP QDRLFTAQID
RSDRFALRYH ALRHQQAQFK SPLRGLRGIR AGLIPHQLHI AKEVGQRLHP RVLLADEVGL
GKTIEAGMIL QQQIFAGRAD RVLIVVPESL QHQWLVEMLR RFNLHFSLFD EERAEDFAAT
DEQEECNPFD SENLIICSLD WLISRPKRRT QALQTQFDLL IVDEAHHLTW SPEAANPEYQ
LVESLTKQIP SVLLLTATPE QLGQESHFAR LKLLDADRFY DYDAFVAEQR HYRPVADAVQ
TLLAENPLSA AEKNAISDLL EEQDLEPLFK ALDSRNEEEK ATVRQELIDS LIDRHGTSRV
LFRNTRQGVK GFPRRIYRQI NLPLPKQYIN AVRVVGRLGK NPEDELFYPE RLFQNMDQNA
KWWDFDPRVE WLITFLKNHR AEKVLVICRQ AQTAVQLEQA LRAKEGIRCA VFHERLSIIE
RDRAAAYFAD QENGAQVLLS SAIGSEGRNF QFACRLVLFN LPENPDLLEQ CIGRLDRIGQ
RRDIRIYVPC FADSPQAVLA DWFHQGLNAF EEICPMGMAL FEKCGQNLQY FLQNPTESAG
FEMFLKKTAE LRLQLKAELE NGRDRLLELN SNGGEAAQRL AEAIRVEDND TELVNFTLNL
FDIIGVEQED SGEKSIVITP TGTMLVPDFP GLKEEGVTVT FDRELALARE ELEFLTWDHP
MLRNGIDLVV SGDIGKTAAS LLVNNKLPTG TLLLELIYVV ESQSPKGLQL NRFLPPTPIR
LLLDGKGQDL AAQVGFNRLE KQLKPMAKNM ASKMVKMVRP NIEKMLSMAE QLMRERAKTL
IGDAQQQADF VLSHELNRLN GLKRVNKNIR QDEIDGLEKI RIRSLSELAK ASWRLDCLRV
IVSNRA
