RAPA_YERE8
ID RAPA_YERE8 Reviewed; 968 AA.
AC A1JJG0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=YE0636;
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(2006).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM286415; CAL10748.1; -; Genomic_DNA.
DR RefSeq; WP_005167013.1; NC_008800.1.
DR RefSeq; YP_001004988.1; NC_008800.1.
DR AlphaFoldDB; A1JJG0; -.
DR SMR; A1JJG0; -.
DR STRING; 393305.YE0636; -.
DR EnsemblBacteria; CAL10748; CAL10748; YE0636.
DR KEGG; yen:YE0636; -.
DR PATRIC; fig|393305.7.peg.729; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OMA; MSILERD; -.
DR Proteomes; UP000000642; 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; Transcription; Transcription regulation.
FT CHAIN 1..968
FT /note="RNA polymerase-associated protein RapA"
FT /id="PRO_1000088399"
FT DOMAIN 164..334
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT DOMAIN 490..664
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 968 AA; 110258 MW; 83848D3663F097F2 CRC64;
MPFTLGQRWI SDTESELGLG TVVAIDVRMV TLLFPATGEN RLYARNDSPI TRVMFNPGDT
ITHHEGWQLK VEEVSEENGL ITYIGTRLDT EETGVSMREV LLDSKLTFSK PQDRLFAGQI
DRMDRFALRF RARKYQSEQF RLPWSGLRGI RASLIPHQLH IAYEVGQRHA PRVLLADEVG
LGKTIEAGMI IHQQLLSGRA ERILIVVPES LQHQWLVEML RRFNLRFSLF DDSRYSEALL
DSTNPFETEQ MVICSLDFVR RNKQRLEQLA DASWDLLVVD EAHHLAWSEE APSREYQVIE
QLAEHIPGVL LLTATPEQLG QQSHFARLRL LDPDRFHDYE EFINEQQKYR PIADAVTLLL
GGERLTDDKL NLLGELINEQ DIEPLLKAAN SQTEDSEAAR QELVTMLMDR HGTSRILFRN
TRNGVKGFPH RVLHQIKLPL PTQYQTAIKV SGIMGAKKSL EARAKDMLYP EQIYQEFEGE
NATWWNFDPR VEWLLNYLIA NRNEKVLVIC AQAATALQLE QVLREREAIR AAVFHEGLSL
IERDRAAAYF ASEEDGAQVL LCSEIGSEGR NFQFACQLVM FDLPFNPDLL EQRIGRLDRI
GQNREIQIMV PYLENTAQAV LVRWYHEGLD AFEHTCPTGR TIYDSGYQEL ITYLATPSEQ
EGLDEFIHTC RQQHEGLKLQ LEQGRDRLLE MHSNGGEHGQ ELAEIIADQD NDVNLVSFAL
NLFDIVGINQ EDRSDNLIVL TPSDHMLVPD FPGLPQDGCT VTFDREQALS REDAQFVSWE
HPIIRNGLDL ILSGDTGSCA VSLLKNKALP VGTLLAELVY VVEAQAPKHL QLTRFLPPTP
VRMLMDKNGT NLAAQVEFES FNRQLNAVNR HTSSKLVNAV QQEVHAMLQQ AEALVEEQAR
LLIEAAKHEA DDKLSAELAR LEALKAVNPN IRDDEIETLE HNRKMVLENL NQAGWRLDAI
RLVVVTHQ
