RAPA_VIBCH
ID RAPA_VIBCH Reviewed; 969 AA.
AC Q9KP70;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=VC_2506;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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; AE003852; AAF95648.1; -; Genomic_DNA.
DR PIR; H82068; H82068.
DR RefSeq; NP_232135.1; NC_002505.1.
DR RefSeq; WP_000006492.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KP70; -.
DR SMR; Q9KP70; -.
DR STRING; 243277.VC_2506; -.
DR DNASU; 2615170; -.
DR EnsemblBacteria; AAF95648; AAF95648; VC_2506.
DR KEGG; vch:VC_2506; -.
DR PATRIC; fig|243277.26.peg.2387; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OMA; MSILERD; -.
DR BioCyc; VCHO:VC2506-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
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..969
FT /note="RNA polymerase-associated protein RapA"
FT /id="PRO_0000207188"
FT DOMAIN 164..334
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT DOMAIN 492..646
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 969 AA; 109440 MW; DF22BEED6F4D7553 CRC64;
MSFALGQRWI SDTESDLGLG TVVALDARTV TLMFAASEEN RVYARSDAPV TRVIFNVGDV
VDSQQGWSLQ VEQVVEDQGV YTYLGTRVDT EESGVALREI FLSNQIRFNK PQDKLFAGQI
DRMDNFVLRY RALTNQYQQH KSPMRGLCGM RAGLIPHQLY IAHEVGRRHA PRVLLADEVG
LGKTIEAGMI IHQQVLTGRA ERILIVVPET LQHQWLVEMM RRFNLHFSIF DEERCVEAFS
EADNPFETQQ YVLCSLDFLR KSRQRFEQAL EAEWDLLVVD EAHHLEWHPE KPSREYQVIE
ALAEQTPGVL LLTATPEQLG RESHFARLRL LDADRFYDYE AFVKEEEQYA PVADAVTALF
SGEKLSDEAK NKITELLSEQ DVEPLFKALE SHASEDEIAL ARQELIDNLM DRHGTGRVLF
RNTRAAIKGF PVRNVHLLPL EIPSQYTTSM RVAGMLGGKL TPEARAMKML YPEEIFQEFE
GEESSWWQFD SRVNWLLEKV KAKRSEKILV IASRASTALQ LEQALREREG IRATVFHEGM
SIIERDKAAA YFAQEEGGAQ VLICSEIGSE GRNFQFANQL VMFDLPFNPD LLEQRIGRLD
RIGQKRDIDV YVPYLTETSQ AILARWFQEG LNAFAETCPT GRAVYDAFAE RLIPILAAGG
GEELEVIIEE SAKLNKTLKS QLEVGRDRLL EMHSNGGEKA QQIAEQIAKT DGDTNLVTFA
LSLFDAIGLH QEDRGENALV VTPAEHMMVP SYPGLPYEGA TITFDRDTAL SREDMHFISW
EHPMVQGGID LLMSEGVGTC AVSLLKNKAL PVGTILLELV YVVDAQAPKR SGISRFLPVS
PIRILMDARG NDLSSQVEFE SFNRQLSPVN RHLASKLVSS VQHDVHRLIT ASETAVEPRV
SAIREQAQRD MQQSLNSELE RLLALKAVNP NIRDEEIEVL DQQIKELTGY IAQAQYQLDS
LRLIVVAHN
