RAPA_KLEP7
ID RAPA_KLEP7 Reviewed; 968 AA.
AC A6T4J7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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};
GN OrderedLocusNames=KPN78578_00570; ORFNames=KPN_00058;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000647; ABR75518.1; -; Genomic_DNA.
DR RefSeq; WP_004177426.1; NC_009648.1.
DR AlphaFoldDB; A6T4J7; -.
DR SMR; A6T4J7; -.
DR STRING; 272620.KPN_00058; -.
DR jPOST; A6T4J7; -.
DR EnsemblBacteria; ABR75518; ABR75518; KPN_00058.
DR KEGG; kpn:KPN_00058; -.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OMA; MSILERD; -.
DR Proteomes; UP000000265; 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..968
FT /note="RNA polymerase-associated protein RapA"
FT /id="PRO_1000088363"
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; 109615 MW; 3FF4EEA9481D4234 CRC64;
MPFTLGQRWI SDTESELGLG TVVALDARMV TLLFPAIGEN RLYSRNDSPI TRVMFNPGDT
ITSHEGWQLH VDKVNEENGL LSYTGTRLDT QEANVTLREV LLDSKLVFSK PQDRLFAGQI
DRMDRFALRY RARKFQSEQY RMPWSGLRGQ RTSLIPHQLH IAHDVGRRHA PRVLLADEVG
LGKTIEAGMI LHQQLLSGAA ERVLIVVPET LQHQWLVEML RRFNLRFSLF DDERYAEAQH
DAYNPFETEQ LVICSLDFVR RSKQRLEHLC DAEWDLMVVD EAHHLVWSEE APSREYQAIE
QLAERVPGIL LLTATPEQLG MESHFARLRL LDPNRFHDFE QFVEEQQNYR PVADAVALLL
AGNKLSDSEL NTLGDLIGEQ DIEPLLQAAN SDREDAQAAR QELISMLMDR HGTSRVLFRN
TRNGVKGFPK RELHTIRLPL PTQYQTAIKV SGIMGARKTA EERARDMLYP EQIYQEFEGD
TGTWWNFDPR VEWLMGYLTS HRSQKVLVIC AKAATALQLE QVLREREGIR AAVFHEGMSI
IERDRAAAWF AEEDTGAQVL LCSEIGSEGR NFQFASNLVM FDLPFNPDLL EQRIGRLDRI
GQAHDIQIHV PYLEKTAQSV LVRWYHEGLD AFEHTCPTGR TVYDSVHDEL INYLAAPESI
DGFDDLIKSC RQQHDALKAQ LEQGRDRLLE IHSNGGEKAQ ALAESIEEQD DDTSLIAFSM
NLFDIVGINQ DDRGENLIVL TPSDHMLVPD FPGLPEDGCT ITFERDVALS REDAQFITWE
HPLIRNGLDL ILSGDTGSST ISLLKNKALP VGTLLLELIY VVEAQAPKQL QLNRFLPATP
VRMLLDKNGN NLAAQVEFES FNRQLSAVNR HTGSKLVNAV QQDVHAILQQ GEAQIAKAAQ
GLIDAARNEA DEKLTAELSR LEALKAVNPN IRDDELAAIE SNRQQVMDAL AQAGWRLDAL
RLIVVTHQ