ID F9Q9A0_9PAST Unreviewed; 884 AA.
AC F9Q9A0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
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=HMPREF9952_2076 {ECO:0000313|EMBL:EGV05861.1};
OS Haemophilus pittmaniae HK 85.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=1035188 {ECO:0000313|EMBL:EGV05861.1, ECO:0000313|Proteomes:UP000006235};
RN [1] {ECO:0000313|EMBL:EGV05861.1, ECO:0000313|Proteomes:UP000006235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK 85 {ECO:0000313|EMBL:EGV05861.1,
RC ECO:0000313|Proteomes:UP000006235};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JUL-2011) 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:EGV05861.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFUV01000013; EGV05861.1; -; Genomic_DNA.
DR AlphaFoldDB; F9Q9A0; -.
DR STRING; 1035188.HMPREF9952_2076; -.
DR Proteomes; UP000006235; 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; 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 {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|HAMAP-Rule:MF_01821};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01821};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01821};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01821};
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};
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 162..336
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 444..607
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT MOTIF 282..285
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01821"
FT BINDING 175..182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01821"
SQ SEQUENCE 884 AA; 99484 MW; 1BB1322BD16FA69A CRC64;
MSFMPGQRYL SETENNLGLG IVTSIEGRRV QLDFPAAQEN RIYAVAEAPL TRVVLQMGDT
LQHRDNWFGK VIARQEMNGL YFYLTAKTDG GEVIVPESEL SSQFSLHNAK ERLLAGQLDS
SELFALRYRT LLAQQAQFQS PLRGLRGNRA GLIPHQLHIA QEVGNRLRPR VLLADEVGLG
KTIEAGMILQ NQLFAEKIRR VLIIVPENLQ HQWLVEMLRR FNLPFALFDE ERAADFAATE
DSPETNPFES EALIICSLDW LTAYPKRAAQ ALAAGFDCLV VDEAHHLAWS QQQVSPQYAL
VERLAQAIPS VLLLTATPEQ LGEESHFARL RLLDPARFYD FQAFIDEQRQ YRPLADTIQA
LLTKRPLTTQ ESQQLAELLP EMRETLACGL ADGSSAVSAR TALIQALIDR HGTGRVLFRN
TRQNIKGFPQ RHYHPIALSN EAAKIDWLLD FLKNHRQDKI LVICHLAHTA QHLVQVLREK
EGIRAALFHE GMSIVERDRA AAYFAEEEGA QVLVSSAIGS EGRNFQFSHC LVLFDLPPNP
DALEQAIGRL DRIGQQQDID IYQPYIKDSS DELLARWYHE GLDAFERLSP AGMSLFTEFD
IAQRRVTGFA DFSSLLIQTR ERREQLQYEL EQGRDRLLEM NSAGGAQAQA LAQQIAAQDG
EPQLRQLAQQ LFDLIGLEQD ELGEHSLVIQ PTGTMMFADF PGLQEEPMTV TFDRALALAR
EEWLFLTWDH PMIRHGIDLI TANDIGKASM ALLVNKQLPA GTLLMETVFV VEAQAPQGLQ
LGRFLPPTAI RLLLDSKGHD LSAQVSFETL QQKLKPLNKA LAVKMLKTVQ SLLQGLFQQA
EKLLAQPAQQ IIDEALLQAK HDLGAEFERL SALQRVNKIF ARMN
//
