ID A0A1Y1SF80_9GAMM Unreviewed; 962 AA.
AC A0A1Y1SF80;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=RNA polymerase-associated protein RapA {ECO:0000256|HAMAP-Rule:MF_01821};
DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_01821};
DE AltName: Full=ATP-dependent helicase HepA {ECO:0000256|HAMAP-Rule:MF_01821};
GN Name=rapA {ECO:0000256|HAMAP-Rule:MF_01821};
GN ORFNames=ATO7_00525 {ECO:0000313|EMBL:ORE88314.1};
OS Oceanococcus atlanticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Oceanococcus.
OX NCBI_TaxID=1317117 {ECO:0000313|EMBL:ORE88314.1, ECO:0000313|Proteomes:UP000192342};
RN [1] {ECO:0000313|EMBL:ORE88314.1, ECO:0000313|Proteomes:UP000192342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-S10r2 {ECO:0000313|EMBL:ORE88314.1,
RC ECO:0000313|Proteomes:UP000192342};
RA Lai Q., Li G., Shao Z.;
RT "Oceanococcus atlanticus 22II-S10r2 Genome Sequencing.";
RL Submitted (APR-2013) 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:0000256|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:0000256|HAMAP-Rule:MF_01821}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RapA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01821}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORE88314.1}.
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DR EMBL; AQQV01000001; ORE88314.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1SF80; -.
DR STRING; 1317117.ATO7_00525; -.
DR Proteomes; UP000192342; Unassembled WGS sequence.
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; 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; PTHR10799:SF971; RNA POLYMERASE-ASSOCIATED PROTEIN RAPA; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 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 {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|HAMAP-Rule:MF_01821};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01821}; Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01821};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_01821, ECO:0000313|EMBL:ORE88314.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01821};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01821}; Reference proteome {ECO:0000313|Proteomes:UP000192342};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_01821};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW Rule:MF_01821}.
FT DOMAIN 167..349
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 488..639
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT COILED 877..904
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 295..298
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01821"
FT BINDING 180..187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01821"
SQ SEQUENCE 962 AA; 107618 MW; DA9FD7F59A85B936 CRC64;
MTDSVTVFAV GQRWISSTEP ELGLGLVVQA EGRVVQVCFP AADEERAYAA RSAPLSRVQF
RQGEMIHDNQ ERRLKVTDTL ENNGVIIYLC EDEDGKDVLL PEEQLHAVIR LNSPRERLFA
GQIDRLSRYR LRYNTRLHHG VQMQSPVRGL LGPRVQLLPH QIYIAHEVAS RHAPRVLLAD
EVGLGKTIEA GMIVHQQLIS GRASRVLVVV PEALLHQWLV EMLRRFNLRF TILDEARCMA
LEGEASGLQE DDVSADDINP FESAQLVLCG ENFLAADTSR AEQARAAGWD ILVVDEAHHL
AWTPENSSPA YACVERLAEQ VPGLLLLTAT PEQLGRSGHF ARLRLLDPDR YHDLQQFVDQ
EQQYQQISDV LMALRQDNAW QRLSSEQGLR EVLDAYLGTD RVAAVVAEVD GADASAQTVA
LERLTRDLLD RHGTGRVLFR NTRASVKGFP GRELHAWPLS GSQALPADVA LDDQLHPEQV
LGLDDDPRLG WLVEFLKQHR QDKVLLICRS AETVCELEQQ LRLAGCYSGL FHEGMSLLER
DRAAAWFADD EDGVQILLCS EIGSEGRNFQ FARHLILFDL PLDPDLLEQR IGRLDRIGQT
GVIQIHVPYL EGTAQQRLLN WYADGLGAFE SPFQIGQAVI NRYGEALLQA LQAADEQPLQ
SLISDAQSFV AQEQARQEQG RDRLLELNSC QPDKADEWVN MVREYERPGV LAPYMEQVFD
AFGVEHESHS AEAVIARPGN HMHGQHFPAL PEDGLTATFR RDVAMSREDM HFLTWEHPMV
TGAMDMILSG DFGNTALCTV KLGGVAPGTL LVESLFVLGV QAPRALQLER YLPAEPVRLL
RDNLGRDLSE QLPADQLHMI AERVPKQTAH ALVKRAEKVL QSLLDTSEKQ AAALQDELID
AAMNQMRAER DDGLQRLLAL AEVNPNVRQQ EIDQYQAETA QLEERLRAAA LQLDAVRIAI
AT
//
