ID U1SB73_9PAST Unreviewed; 952 AA.
AC U1SB73;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
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=HMPREF9065_00984 {ECO:0000313|EMBL:ERH27877.1};
OS Aggregatibacter sp. oral taxon 458 str. W10330.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Aggregatibacter.
OX NCBI_TaxID=1321772 {ECO:0000313|EMBL:ERH27877.1, ECO:0000313|Proteomes:UP000016531};
RN [1] {ECO:0000313|EMBL:ERH27877.1, ECO:0000313|Proteomes:UP000016531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W10330 {ECO:0000313|EMBL:ERH27877.1,
RC ECO:0000313|Proteomes:UP000016531};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-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:ERH27877.1}.
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DR EMBL; AWSH01000039; ERH27877.1; -; Genomic_DNA.
DR RefSeq; WP_021615139.1; NZ_KE952587.1.
DR AlphaFoldDB; U1SB73; -.
DR STRING; 1321772.HMPREF9065_00984; -.
DR PATRIC; fig|1321772.3.peg.906; -.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OrthoDB; 9814088at2; -.
DR Proteomes; UP000016531; 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; 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 {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|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 474..645
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT COILED 644..671
FT /evidence="ECO:0000256|SAM:Coils"
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 952 AA; 108934 MW; ADADF917AC1847AB CRC64;
MTFAVGQRWI SETENNLGLG VIRAVDFRQV TIDFPAAQEQ RIYSVQNAPL NRVQFRIGDL
IQHVEGWHGE VLNVAENNGL LFYLVQQEGK EDRVVSEMDL AHRISFCRPQ ERLFSAQIDR
NDHFVLRYQA LQYQKAQFQS PLRGLRGIRA GLIPHQLHIA KEAGQRIAPR VLLADEVGLG
KTIEAGMILQ QQLFAEKVRR VLVIVPETLQ HQWLVEMLRR FNLHFSLFDE ERCADFATTE
EQEEVNPFTT ESLIICALDW LVQHPQRVQQ LLAAEFDMLI ADEVHHLVYD EVNPSLEYQL
VQQLTQHIPA VLLLTATPEQ LGQQSHFARL NLLDPHRFHN YHAFLEEQQH YQPIAEAAQA
LLADKPLSAV EKNTISALLG EEINFNGTNK ETLIKQLIDR HGTGRLLFRN TRQSVQGFPK
RIYHPIALLQ PKQYENAVKT LRALGEHPVQ CALYPEHFMR ELNANTSWWE FDLRVQWLID
FLKQHRQEKV FVICSYAGTA IQLEQILREK EGIRSAVFHE KMAIVERDRA AAYFAQQENG
AQVLLSSNIG SEGRNFQFAS RLVLFNLPEN PDLLEQCIGR LDRIGQTKDI QIYLPYFTDS
AQAVLADWYH LGLNAFNETC PMGALLFEQF GEALQKTLEN PTALDAQNAL IDHTQQERLR
LKQQLEQGRD LLLELNSNGG EPAKQLAQEI AAQDGSPELV DFSLNLFDVI GVEQEDLGEK
SIVITPTGTM LVPEFPGLKE EGVTVTFDRQ LALAREELEF LTWDHPMIYH GIDLITSSDI
GKSAVALLPN KHLPAGTLLL ELVYVVETQA PQGLQLTRFL PPTPIRLLLD SKGNDLAQQV
AFDHFQRKLK PMDRNMANKV VKMLRPNIER LITQGEKVMA QQSKAIIANA EQQALQHLDE
ELTRLIALRK VNKNIRQDEI DTLQMQRQQM RQCLQQATWR LDCLRVIVTN KE
//
