RAPA_ALISL
ID RAPA_ALISL Reviewed; 969 AA.
AC B6EPV7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=VSAL_I0352;
OS Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS LFI1238)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=316275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LFI1238;
RX PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT LFI1238 shows extensive evidence of gene decay.";
RL BMC Genomics 9:616-616(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; FM178379; CAQ78037.1; -; Genomic_DNA.
DR RefSeq; WP_012549180.1; NC_011312.1.
DR AlphaFoldDB; B6EPV7; -.
DR SMR; B6EPV7; -.
DR STRING; 316275.VSAL_I0352; -.
DR EnsemblBacteria; CAQ78037; CAQ78037; VSAL_I0352.
DR KEGG; vsa:VSAL_I0352; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OMA; MSILERD; -.
DR OrthoDB; 291634at2; -.
DR Proteomes; UP000001730; 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; Transcription; Transcription regulation.
FT CHAIN 1..969
FT /note="RNA polymerase-associated protein RapA"
FT /id="PRO_1000188167"
FT DOMAIN 164..334
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT DOMAIN 492..672
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; 109198 MW; C9C6F6092E398CEC CRC64;
MSFALGQRWI SDTESDLGLG TVVAVDDRTV SVLFAASEEN RLYAKHDAPI TRVTFNKGDT
IESHEGWSLE VEDVIEDGGL LTYIGTRTDT DEVNVVLRET LLSHQIRFNK PQDKLFAGQI
DRMDRFALRF RALQNQYEQH KNPMRGLCGM RAGLIPHQLF IAHEVGRRYA PRVLLADEVG
LGKTIEAGMI IHQQVLSGRA ERVLIVVPET LQHQWLVEMM RRFNLHFSIF DEERCIESYA
DSENPFDTAQ LVLCSLDFIR RSKRRFEQVV EADWDLLVVD EAHHLEWNQT KPSRAYQVIE
AIAEETAGVL LLTATPEQLG HESHFARLRL LDPDRFYDYD AFVEEERQYQ PVADAVTALM
SGDKLSNDAK NRIAELLSEQ DVEPLFRIIE SDGSEEQQSQ VRQELVDNLM DRHGTGRVLF
RNTRAAIKGF PQRNLNLMPM ALPPQYATSM RVATMMGGRM SNEARAMKML YPEEIFQEFE
GDSATWWQFD PRVNWLLELL KENRNEKVLI IASRASTALQ LEQALREREG IRGTVFHEGM
SIIERDKAAA YFAQEEGGAQ VLICSEIGSE GRNFQFANQL VMFDLPFNPD LLEQRIGRLD
RIGQKRDIDI HVPYLQGTSQ ELLARWFDEG LNAFGETCPT GRAVYEKFSD TIIAILATGK
SDGLEPLIEE SAALNKELKA QLEQGRDRLL EVHSNGGNKA KELAEKIAAT DGDIHLVNFA
LNLFDTIGLN QDDKGENAIV VTPAENMLVS SYPGLPYEGC TITFDRKTAL SREDMNLISW
EHPMIQGGID LVLTEGVGAT AVSLLKNKAL PAGTLLLELI YVVDAQAPKK SGIGRFLPKT
PIRLMMDSKG NDLSAQVEFE SFNRQLSPVN RHMASKLVNS VQKEIHALID TAEVSIEDRI
EAVRVDANAE MKTALNGELD RLQALKAVNP NIRDEELTQI ETQMSELSAY IGKAQVQLDS
LRLIVVSHN
