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

Autoinhibited structure

Activated structure

6 structures for P60240

Entry ID Method Resolution Chain Position Source
4S20 X-ray 470 A K/L 1-968 PDB
6BOG X-ray 320 A A/B 1-968 PDB
7M8E EM 340 A F 1-968 PDB
7MKN EM 330 A L 1-968 PDB
7MKQ EM 480 A L 1-968 PDB
AF-P60240-F1 Predicted AlphaFoldDB

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

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