P60240
Gene name |
rapA (hepA, yabA, b0059, JW0058) |
Protein name |
RNA polymerase-associated protein RapA |
Names |
ATP-dependent helicase HepA |
Species |
Escherichia coli (strain K12) |
KEGG Pathway |
ecj:JW0058, eco:b0059, |
EC number |
|
Protein Class |
DNA ANNEALING HELICASE AND ENDONUCLEASE ZRANB3 FAMILY MEMBER (PTHR45766) |

Descriptions
RapA, a bacterial RNA polymerase-associated Swi2/Snf2 ATPase, has its ATPase activity autoinhibited by its N-terminal domain (NTD) but is activated upon binding with RNA polymerase (RNAP). This activation involves the structural remodeling of the ATPase active site in RapA, where the NTD of RapA is wedged open by the RNAP β’ zinc-binding domain (ZBD), and the RNAP β flap tip helix (FTH) forms extensive hydrophobic interactions with the RapA ATPase core domains. This interaction facilitates the suppression of the autoinhibitory effect of the NTD and enhances the ATPase activity of RapA, crucial for stimulating RNAP recycling.
Autoinhibitory domains (AIDs)
Target domain |
177-602 (ATPase domain) |
Relief mechanism |
Partner binding |
Assay |
Structural analysis |
Accessory elements
No accessory elements
References
No variants for P60240
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
No variants for P60240 |
No associated diseases with P60240
No regional properties for P60240
Type | Name | Position | InterPro Accession |
---|---|---|---|
No domain, repeats, and functional sites for P60240 |
Functions
Description | ||
---|---|---|
EC Number | ||
Subcellular Localization |
|
|
PANTHER Family | PTHR45766 | DNA ANNEALING HELICASE AND ENDONUCLEASE ZRANB3 FAMILY MEMBER |
PANTHER Subfamily | PTHR45766:SF3 | SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A-LIKE PROTEIN 1 |
PANTHER Protein Class | DNA metabolism protein | |
PANTHER Pathway Category |
Wnt signaling pathway SWI/SNF |
1 GO annotations of cellular component
Name | Definition |
---|---|
cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
7 GO annotations of molecular function
Name | Definition |
---|---|
ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
ATP hydrolysis activity | Catalysis of the reaction |
ATP-dependent chromatin remodeler activity | An activity, driven by ATP hydrolysis, that modulates the contacts between histones and DNA, resulting in a change in chromosome architecture within the nucleosomal array, leading to chromatin remodeling. |
bacterial-type RNA polymerase core enzyme binding | Binding to a bacterial-type RNA polymerase core enzyme, typically consisting of two alpha, one beta, one beta prime, and one omega subunit. |
DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
helicase activity | Catalysis of the reaction |
nucleic acid binding | Binding to a nucleic acid. |
1 GO annotations of biological process
Name | Definition |
---|---|
positive regulation of DNA-templated transcription | Any process that activates or increases the frequency, rate or extent of cellular DNA-templated transcription. |
No homologous proteins in AiPD
UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
---|---|---|---|---|
No homologous proteins |
10 | 20 | 30 | 40 | 50 | 60 |
MPFTLGQRWI | SDTESELGLG | TVVAVDARTV | TLLFPSTGEN | RLYARSDSPV | TRVMFNPGDT |
70 | 80 | 90 | 100 | 110 | 120 |
ITSHDGWQMQ | VEEVKEENGL | LTYIGTRLDT | EESGVALREV | FLDSKLVFSK | PQDRLFAGQI |
130 | 140 | 150 | 160 | 170 | 180 |
DRMDRFALRY | RARKYSSEQF | RMPYSGLRGQ | RTSLIPHQLN | IAHDVGRRHA | PRVLLADEVG |
190 | 200 | 210 | 220 | 230 | 240 |
LGKTIEAGMI | LHQQLLSGAA | ERVLIIVPET | LQHQWLVEML | RRFNLRFALF | DDERYAEAQH |
250 | 260 | 270 | 280 | 290 | 300 |
DAYNPFDTEQ | LVICSLDFAR | RSKQRLEHLC | EAEWDLLVVD | EAHHLVWSED | APSREYQAIE |
310 | 320 | 330 | 340 | 350 | 360 |
QLAEHVPGVL | LLTATPEQLG | MESHFARLRL | LDPNRFHDFA | QFVEEQKNYR | PVADAVAMLL |
370 | 380 | 390 | 400 | 410 | 420 |
AGNKLSNDEL | NMLGEMIGEQ | DIEPLLQAAN | SDSEDAQSAR | QELVSMLMDR | HGTSRVLFRN |
430 | 440 | 450 | 460 | 470 | 480 |
TRNGVKGFPK | RELHTIKLPL | PTQYQTAIKV | SGIMGARKSA | EDRARDMLYP | ERIYQEFEGD |
490 | 500 | 510 | 520 | 530 | 540 |
NATWWNFDPR | VEWLMGYLTS | HRSQKVLVIC | AKAATALQLE | QVLREREGIR | AAVFHEGMSI |
550 | 560 | 570 | 580 | 590 | 600 |
IERDRAAAWF | AEEDTGAQVL | LCSEIGSEGR | NFQFASHMVM | FDLPFNPDLL | EQRIGRLDRI |
610 | 620 | 630 | 640 | 650 | 660 |
GQAHDIQIHV | PYLEKTAQSV | LVRWYHEGLD | AFEHTCPTGR | TIYDSVYNDL | INYLASPDQT |
670 | 680 | 690 | 700 | 710 | 720 |
EGFDDLIKNC | REQHEALKAQ | LEQGRDRLLE | IHSNGGEKAQ | ALAESIEEQD | DDTNLIAFAM |
730 | 740 | 750 | 760 | 770 | 780 |
NLFDIIGINQ | DDRGDNMIVL | TPSDHMLVPD | FPGLSEDGIT | ITFDREVALA | REDAQFITWE |
790 | 800 | 810 | 820 | 830 | 840 |
HPLIRNGLDL | ILSGDTGSST | ISLLKNKALP | VGTLLVELIY | VVEAQAPKQL | QLNRFLPPTP |
850 | 860 | 870 | 880 | 890 | 900 |
VRMLLDKNGN | NLAAQVEFET | FNRQLNAVNR | HTGSKLVNAV | QQDVHAILQL | GEAQIEKSAR |
910 | 920 | 930 | 940 | 950 | 960 |
ALIDAARNEA | DEKLSAELSR | LEALRAVNPN | IRDDELTAIE | SNRQQVMESL | DQAGWRLDAL |
RLIVVTHQ |