RAPA_YERPS
ID RAPA_YERPS Reviewed; 968 AA.
AC Q66EN4;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, 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}; Synonyms=hepA;
GN OrderedLocusNames=YPTB0658;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH19898.1; -; Genomic_DNA.
DR RefSeq; WP_011191719.1; NZ_CP009712.1.
DR AlphaFoldDB; Q66EN4; -.
DR SMR; Q66EN4; -.
DR EnsemblBacteria; CAH19898; CAH19898; YPTB0658.
DR GeneID; 66842921; -.
DR KEGG; ypo:BZ17_1899; -.
DR KEGG; yps:YPTB0658; -.
DR PATRIC; fig|273123.14.peg.2018; -.
DR OMA; MSILERD; -.
DR Proteomes; UP000001011; 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_0000207193"
FT DOMAIN 164..334
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT DOMAIN 490..644
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; 110109 MW; F9EA8B6618871DC4 CRC64;
MPFTLGQRWI SDTESELGLG TVVAIDVRMI TLLFPATGEN RLYARNDSPI TRVMFNPSDT
ITHHEGWQLK VEEVTQENGL ITYIGTRLDT EETGVAMREV LLDSKLTFSK PQDRLFAGQI
DRMDRFALRF RARKYQSEQF RLPWSGLRGI RASLIPHQLH IAYEVGQRHA PRVLLADEVG
LGKTIEAGMI IHQQLLAGRA ERVLIVVPES LQHQWLVEML RRFNLRFSLF DDSRYSEALL
DSSNPFDTEQ MVICSLDFVR RNKQRLEQLA DASWDLLVVD EAHHLAWSEE APSREYQVIE
QLAEHIPGVL LLTATPEQLG QQSHFARLRL LDPDRFHDYE EFVNEQQKYR PIADAVTLLL
GGERLTDDKL NLLGELIDEQ DIEPLLKAAN SQSEDSEAAR QELVTMLMDR HGTSRVLFRN
TRNGVKGFPH RVLHQIKLPL PTQYQTAIKV SGIMGAKKTL DARAKDMLYP EQIYQEFEGE
NATWWNFDPR VEWLLNYLVA NRGEKVLVIC AQAATALQLE QVLREREAIR AAVFHEGLSL
IERDRAAAYF ASEEDGAQVL LCSEIGSEGR NFQFACQLVM FDLPFNPDLL EQRIGRLDRI
GQNREIQIMV PYLEDTAQAI LVRWYHEGLD AFEHTCPTGR TIYDSSYQEL ISYLATPSEQ
EGLDEFIHTC RQQHEGLKLQ LEQGRDRLLE MHSNGGEHGQ ELAQSIAEQD NDINLVSFAL
NLFDIVGINQ EDRSDNLIVL TPSDHMLVPD FPGLPPDGCT VTFDREQALS REDAQFVSWE
HPIIRNGLDL ILSGDTGSCA VSLLKNKALP VGTLLAELVY VVEAQAPKHL QLTRFLPPTP
VRMLMDRNGT NLAAQVEFES FNRQLNAVNR HTSSKLVNAV QQEVHTMLQQ AEALVEAQAQ
ALIETAKREA DDKLSTELAR LEALKAVNPN IRDDEIEALE HNRKMVLENL NQAGWRLDAI
RLVVVTHQ
