ID RAPA_SHEAM Reviewed; 967 AA.
AC A1SAC7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
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=Sama_3131;
OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=326297;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1098 / SB2B;
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 Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA Richardson P.;
RT "Complete sequence of Shewanella amazonensis SB2B.";
RL Submitted (DEC-2006) 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; CP000507; ABM01334.1; -; Genomic_DNA.
DR RefSeq; WP_011761238.1; NC_008700.1.
DR AlphaFoldDB; A1SAC7; -.
DR SMR; A1SAC7; -.
DR STRING; 326297.Sama_3131; -.
DR KEGG; saz:Sama_3131; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OrthoDB; 9814088at2; -.
DR Proteomes; UP000009175; 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 DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd18011; DEXDc_RapA; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 2.30.30.930; -; 1.
DR Gene3D; 3.30.360.80; -; 1.
DR Gene3D; 6.10.140.1500; -; 1.
DR Gene3D; 6.10.140.2230; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 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; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR040765; Tudor_1_RapA.
DR InterPro; IPR040766; Tudor_2_RapA.
DR PANTHER; PTHR45766; DNA ANNEALING HELICASE AND ENDONUCLEASE ZRANB3 FAMILY MEMBER; 1.
DR PANTHER; PTHR45766:SF3; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A-LIKE PROTEIN 1; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 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..967
FT /note="RNA polymerase-associated protein RapA"
FT /id="PRO_1000088377"
FT DOMAIN 163..332
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT DOMAIN 491..639
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 967 AA; 108828 MW; BB8E3CBF820F5EAC CRC64;
MSFAVGQRWI SDTESELGLG TVVQIEGRMV TLLFPATGEN RMFAMAEAPL TRVIYNPGDT
IDSAEGWGMT VDKVEELNGL VFYLGKRTDT GEDTMLRETL LEHNIRFNKP QDRLYAGQID
RIERFGVRYK AQLLRHKQAT SPLLGLQGPR VGLIPHQLWI AHEVGRRHAP RVLLADEVGL
GKTIEAGLII HQQLMTGRAE RVLVIVPDTL RHQWLVEMLR RFNLRFSVFD EDRCVEAFAD
HDNPFYTEQL VICSLELLRK KRRLEQALDA DWDLMVVDEA HHLEWSEDEP SRAYQVVEAL
AEVVPGVLLL TATPDQLGHQ SHFARLRLLD PDRFYDYQAF LDEEKGYQAV AEAADALASG
IKLSDEAING LTELLSEKDI APAIRQIQAE NLDEELRQAA RDELLQELLD RHGTGRVLFR
NSRASVKGFP KREFHSHGFE LPEQYVTAMR VNAMMGGART QEARVAQALS PERIYQEFDD
NNASWWKFDP RVDWLIDFLK SHRSKKVLVI ASRAETALAL EEALRTREGI QATVFHEGMS
IIERDKAGAY FAQEEGGAQA LICSEIGSEG RNFQFASQLV LFDLPLNPDL LEQRIGRLDR
IGQRHDVQIH LPFLKHTAQE QLMHWYHEGL CAFELTCPGG HVLFGEFKER LLSVLTGESD
ELDELMADTK ARYKALKAAM EQGRDKLLEL NSHGGAKAEA ITASLSDADE DTDLIASVIR
LWDVIGIDQD DKGENSIVLR TTEHMMYPTY PGLNEDGVTV TFDRNTALSR DDIALITLEH
PLVQTGLDLI TGSDTGTTCV ALLKNKALPA GTIFLELIYL AETTAPKASQ LYRYLPPTPV
RVLLDKNGNN LSDKVDYDSF DKQLSGVNRH IASKLVNASQ TMLHPLFAKG EEFAGEALET
LTQDARARME SQLGAELSRL EALKAVNPSI REEELEHLRN MMQELSGYLG NTQLKLDAIR
LVLVSHN
//
