ID G9ELA4_9GAMM Unreviewed; 967 AA.
AC G9ELA4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=LDG_6165 {ECO:0000313|EMBL:EHL31993.1};
OS Legionella drancourtii LLAP12.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=658187 {ECO:0000313|EMBL:EHL31993.1, ECO:0000313|Proteomes:UP000002770};
RN [1] {ECO:0000313|EMBL:EHL31993.1, ECO:0000313|Proteomes:UP000002770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LLAP12 {ECO:0000313|EMBL:EHL31993.1,
RC ECO:0000313|Proteomes:UP000002770};
RX PubMed=22047552; DOI=10.1186/1471-2164-12-542;
RA Gimenez G., Bertelli C., Moliner C., Robert C., Raoult D., Fournier P.E.,
RA Greub G.;
RT "Insight into cross-talk between intra-amoebal pathogens.";
RL BMC Genomics 12:542-542(2011).
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 ---------------------------------------------------------------------------
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; JH413808; EHL31993.1; -; Genomic_DNA.
DR RefSeq; WP_006870104.1; NZ_JH413808.1.
DR AlphaFoldDB; G9ELA4; -.
DR STRING; 658187.LDG_6165; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_011520_0_0_6; -.
DR InParanoid; G9ELA4; -.
DR OrthoDB; 9814088at2; -.
DR Proteomes; UP000002770; 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};
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}; Reference proteome {ECO:0000313|Proteomes:UP000002770};
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..356
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 490..651
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT MOTIF 302..305
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 967 AA; 109692 MW; 07855B35AA00C830 CRC64;
MTFCIGQRWI SNTESQLGLG IITELSGRQV HISFPAAGEE RIYATDNAPL SRIIYKADDE
IITSNQQKVR LTQIDEHQGL FFYTGVDEQG EEIRISEVGL NCFITLNTPQ QRLFSGLLDK
LNSYRLRIDT LNHASRLQQS NVRGLLGSRT SHLPHQVYIA REVAQRHAPR VLLADEVGLG
KTIEAGMILH YQLCTGRANR VLIVVPQTLI HQWLVEMIRR FNLHFSIIDA SRYKPLHDNY
GEDDDYDLDD EDELDAAEEV TVNNASPFAT ESLVLCSLDF LMDHDEARAH ALACDWDLLI
VDEAHHLHWS EQEQSPEYEC IEGLSAQSKG LLLLTATPEQ AGIASHFARL RLLDPSRYYD
FSAFKQEEAG YQKINQLVQE LLAYDADTAL NALDPALKQQ VDSYLGDAQG STIQESIKNL
LDRHGTGRVL FRNTRAAIQG FPARHVHSYP LARPEIYSLL TEQSGLINLS PENSFSNKEL
WLDKDPRVAW LANKIIELYP NKVLVICAKA KTAIALEHYF KLKAGIRSAA FHESLTIIER
DRAAAYFAEQ ENGAQALICS EIGSEGRNFQ FAHHLVLFDL PINPDLLEQR IGRLDRIGQA
HDIEIHVPYL ANTAQEKLFR WYHEGFNLFN KSCSVGFTLY EEFEPRLLPI LDQAQSAASD
GLLAQLIADT KARVEQINQA LHDGRDRLLE MNSCNAPQAE ALIAEIEVEE YCLDLENYMA
QIFHEYGIDH EYHSEATEIL QPTEHMKTGH FPCLKEEGVT VTYSRLKALQ REDMEFLSWE
HPMVTESMEM ILDSEVGNAA LATISIKSIP AGTVFLESFF TVNCAAPKYL QLDRFLPLTP
IRLFMDVSGK NLTKVLDYAR LNQLCQSVKR HLGYPIIKQI HKEIENILVY SKHAAEGQLS
DIIAQAKAHM RKSISHEVQR LEALQALNPG IRDDEIAFFK QQLQDSEHYM NNAVLQLQAL
RVIVNKH
//
