RAPA_VIBC3
ID RAPA_VIBC3 Reviewed; 969 AA.
AC A5F5C5; C3M4Z5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=VC0395_A2088, VC395_2620;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
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; CP000627; ABQ19970.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP10606.1; -; Genomic_DNA.
DR RefSeq; WP_000006481.1; NZ_JAACZH010000021.1.
DR AlphaFoldDB; A5F5C5; -.
DR SMR; A5F5C5; -.
DR STRING; 345073.VC395_2620; -.
DR EnsemblBacteria; ABQ19970; ABQ19970; VC0395_A2088.
DR KEGG; vco:VC0395_A2088; -.
DR KEGG; vcr:VC395_2620; -.
DR PATRIC; fig|345073.21.peg.2522; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OMA; MSILERD; -.
DR Proteomes; UP000000249; Chromosome 2.
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..969
FT /note="RNA polymerase-associated protein RapA"
FT /id="PRO_1000088397"
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; 109380 MW; 3C7F9E30BED95982 CRC64;
MSFALGQRWI SDTESDLGLG TVVALDARTV TLMFAASEEN RVYARSDAPV TRVIFNVGDV
VDSQQGWSLQ VEQVVEDQGV YTYLGTRVDT EESGVALREI FLSNQIRFNK PQDKLFAGQI
DRMDNFVLRY RALANQYQQH 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
GDESSWWQFD 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 ASEAAVEPRV
SAIREQAQRD MQQSLNSELE RLLALKAVNP NIRDEEIEVL EQQIKELTGY IAQAQYQLDS
LRLIVVAHN
