RAPA_HAEIN
ID RAPA_HAEIN Reviewed; 923 AA.
AC P44781;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 127.
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=HI_0616;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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; L42023; AAC22275.1; -; Genomic_DNA.
DR PIR; H64081; H64081.
DR RefSeq; NP_438774.1; NC_000907.1.
DR RefSeq; WP_005692755.1; NC_000907.1.
DR AlphaFoldDB; P44781; -.
DR SMR; P44781; -.
DR STRING; 71421.HI_0616; -.
DR EnsemblBacteria; AAC22275; AAC22275; HI_0616.
DR KEGG; hin:HI_0616; -.
DR PATRIC; fig|71421.8.peg.640; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OMA; MSILERD; -.
DR PhylomeDB; P44781; -.
DR BioCyc; HINF71421:G1GJ1-637-MON; -.
DR Proteomes; UP000000579; 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..923
FT /note="RNA polymerase-associated protein RapA"
FT /id="PRO_0000207177"
FT DOMAIN 162..332
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT DOMAIN 443..597
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT MOTIF 278..281
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 923 AA; 104405 MW; 8022403581DAADBD CRC64;
MPFAIGQRWL SESENALGLG VITALDQRTV TIYFPAADET RIYAMAQAPL SRIVFSKGET
LSHQAGWQGE ILDVQNMNGL LFYLVKNPQD EDVIVQERDI SPIISFSQAK DRLFSAQIDR
STHFALRYRT LCHQQAQFKS PLRGLRGTRA SLIPHQLHIA AEVGNRVNPR VLLADEVGLG
KTIEAGMILQ NQLFAEKVQR VLIIVPETLQ HQWLVEMLRR FNLHFALFDE ERCNDFDLDA
VNPFTTESLI ICSLNWLETH PNRVELVLNA QFDCLIVDEA HHLVWSETSP STAYLLVEQL
ARIIPSVLLL TATPEQLGQE SHFARLRLLD PERFFDYQTF VKEQEHYQPV VNAVESLLAN
KALSAVEKNH ISDLLLEQDV EPLFKAIASN NDEEQQRARQ ELIQALIDRH GTGRMLFRNT
RQGVKGFPHR VYHQITLSEE NDKIDWLIDF LKLHRNEKIF VICQTAATAI QLEQILRERE
AIRAAVFHEK MSIIERDRAA AYFADLENGA QVLLSSSIGS EGRNFQFAAN LVLFDLPTNP
DLLEQCIGRL DRIGQKRDVQ VYVPCAKDSP QSRLARWYNE GLNAFEQTCP MGMALFSQFA
DELEKVRSNS TALSENEFSG LLKQTKTARE KLKIELEKGR DRLLELNSHG GEQAQALADQ
IADEDNSPEL VNFALKLFDI IGVEQEDLGA NSIVISPTGT MLVPDFPGLK EEGVTVTFDR
ELALAREEME FLTWDHPMIR QGIDLVASGD IGKAAMALLV NKQLPAGTLL IELIYVVESQ
SPKGLQLNRF LPPTPIRLLL DNKGNNIGEQ VAFETLHSKL KPLGKNITNQ MVKMARSNIE
SLIMRGDQLV KSLAEPIIAE AKNQADQQLS AEINRLQALR AVNKNIRQSE IDILEQQRTQ
SLDELSKANW RLDCLRVIVT NKE
