RAPA_SHELP
ID RAPA_SHELP Reviewed; 968 AA.
AC A3QA31;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=Shew_0457;
OS Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=323850;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1088 / PV-4;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA Fredrickson J., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella loihica PV-4.";
RL Submitted (MAR-2007) 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; CP000606; ABO22329.1; -; Genomic_DNA.
DR RefSeq; WP_011864263.1; NC_009092.1.
DR AlphaFoldDB; A3QA31; -.
DR SMR; A3QA31; -.
DR STRING; 323850.Shew_0457; -.
DR PRIDE; A3QA31; -.
DR EnsemblBacteria; ABO22329; ABO22329; Shew_0457.
DR KEGG; slo:Shew_0457; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OMA; MSILERD; -.
DR OrthoDB; 291634at2; -.
DR Proteomes; UP000001558; 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_1000088384"
FT DOMAIN 163..332
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT DOMAIN 491..645
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT MOTIF 278..281
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 968 AA; 109620 MW; B17A4E66667A9EA9 CRC64;
MPFSLGQRWI SDTESELGLG TVIGLEGRMV TLMFPATDEN RMFARDDAPL TRVIYNPGDI
IESHEGWSLK VSEIEEKNQL VIYHGIHTET GEEVSLRETL LNHNIRFNKP QDRLFAGQID
RLDRFGVRYQ SQLLRHKLAT SDLLGLQGPR VGLIPHQQWI AHEVGQRFAP RVLLADEVGL
GKTIEAGLII HQQLLTGRAE RILIIVPDTL RHQWLVEMLR RFNLRFSVFD EDRCVEAYAD
HDNPFYTEQL VICSLELLRK KKRLDQALDA DWDLMVVDEA HHLEWTEEEP SRAYRVVEAL
SEVVPGVLLL TATPDQLGHQ SHFARLRLLD PDRFYDYQAF LKEEESYKEV ASAADALASG
KRLPDEAVAS LTELLNEKDI TPALRLIEDE SVDNEQRDQA RSELLQELLD RHGTGRVLYR
NSRASVKGFP TRIFNAHPQT MPAQYKTAAR VSDMMGGQTD LTAKVKQALS PEKLYQAFES
DSASWWKFDP RVDWLIDFLK NHRSKKVLII ASQAETALSL EEALRTREGI QATVFHEGMS
IIERDKAGAY FAQESGGAQA LICSEIGSEG RNFQFASHLV LFDLPLNPDL LEQRIGRLDR
IGQANDVEIH LPYLANTAQE NLMNWYHKGL NAFEQTCPTG HILFNEFSEE LLTQLVYRDE
DKFTQLLNHT QSRYKALKKA MEQGRDKLLE INSHGGDKAQ KLVENLAARD QDTQLIGSVI
RLWDIIGVEQ EDSGENAIVL HPSEHMMFPT YPGLPEDGIT VTFDREMALS RDDIALITQE
HPLVQTGLDL ITSSETGTTS VAVLKNKALP AGTIFLELIY MADASAPRSS QLYRYMPPTP
VRVLLDKNGN NLSQNVSYES FDKQLSAVNR HIASKLVNAS QTLLHPLFAK GEEFAQAAMK
QLTEEASNKM TQQLTAELER LEALKAVNPN IRDEELEHLR NQMVELGNYL DACQLQLDAV
RLVLVSHA