RAPA_AERHH
ID RAPA_AERHH Reviewed; 955 AA.
AC A0KGL5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=AHA_0864;
OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=380703;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC
RC 2358 / NCIMB 9240 / NCTC 8049;
RX PubMed=16980456; DOI=10.1128/jb.00621-06;
RA Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H.,
RA Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL J. Bacteriol. 188:8272-8282(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}.
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DR EMBL; CP000462; ABK36250.1; -; Genomic_DNA.
DR RefSeq; WP_011704808.1; NC_008570.1.
DR RefSeq; YP_855406.1; NC_008570.1.
DR AlphaFoldDB; A0KGL5; -.
DR SMR; A0KGL5; -.
DR STRING; 380703.AHA_0864; -.
DR EnsemblBacteria; ABK36250; ABK36250; AHA_0864.
DR KEGG; aha:AHA_0864; -.
DR PATRIC; fig|380703.7.peg.868; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OMA; MSILERD; -.
DR Proteomes; UP000000756; 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..955
FT /note="RNA polymerase-associated protein RapA"
FT /id="PRO_1000088348"
FT DOMAIN 163..333
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT DOMAIN 478..642
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT MOTIF 279..282
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 955 AA; 107271 MW; 057A0606A509B8DB CRC64;
MPFALGQRWI SDTETDLGLG TVVAVEGRMV TLLFPATGEN RMYAKEEAPV TRVSFNVGDQ
IASHEDWTMT VEEVQEKDGL LIYVGVRTDN DEPVALKEVF LNNFIKFNKP QDRLFAGQID
RMSRFTLRYE ALINQHQRRR NPTRGLAGGR VSLIPHQLYI AHEVGHRYAP RVLLADEVGL
GKTIEAGMII HQQLLSGRAH RVLILLPETL QHQWLVEMLR RFNLHFSLFD EERCIEAFAD
AENPFETEQL VICSLDFLRK KRRRFEQVLE AEWDLLVVDE AHHLEWSEEA PSRAYEMVEA
LAEQVPGVLL LTATPDQLGH QSHFARLRLL DPERFYDYDA FLAEEQAYGQ VASAAQELLD
GETLSDEAKR ILASQLEGLD LSDAAARQQA VAKLLDQHGT GRVLFRNSRA NIQGFPERHL
NVYPMPLPEQ YKTAIKVMGM MGGNGGDLQT RALRYLYPEK IFQQFEGDNA TWTQFDPRVE
WLLELLLSAR QQKVLVICSE AATAIALEEA LRTREGIRGA VFHEGMSILE RDKASAYFAQ
QEGGAQVLLC SEIGSEGRNF QFASHLVLFD LPLNPDLLEQ RIGRLDRIGQ QNTVEIHVPY
LEGTSQRALQ LWYHDGLDAF EQTCPTARPV FEAVRDELFE LLAANTGDQA PLDALLVKTR
ELHEPLKARL EQGRDRLLEI HSSGGAAAQQ LVDKLAAEDD DTGMISFALK MFDEIGVNQD
DRGENALVLT PGDHMLVSSF PGLPQDGMTI TFDRNTALSR DDMALLSWDH PMMRGGIDLI
LGSEIGATSV ALLKNKALPI GSILLELIFV AESAAHPQLY RFMPPTPIRL LMDKNGQNLG
EKVAFDAFNR QLTPVNRHLG SKLVTASQPV IHGLIGKGQA IAEELKGGIV DKARAQMAQT
LQQDLDRLEA LKAVNPNVRD SELDYLRNLQ AELHHLIDQT QLKLDAIRFI VVTHN
