P30958
Gene name |
mfd (b1114, JW1100) |
Protein name |
Transcription-repair-coupling factor |
Names |
TRCF |
Species |
Escherichia coli (strain K12) |
KEGG Pathway |
ecj:JW1100, eco:b1114, |
EC number |
|
Protein Class |
ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC (PTHR47964) |

Descriptions
Mfd has little motor activity in isolation but exhibits efficient oligonucleotide displacement activity when bound to a stalled transcription complex. Deletion of the C-terminal domain of Mfd increases the ATPase activity of the protein and allows efficient oligo displacement in the absence of RNAP, suggesting that an autoinhibitory element ensures the motor activity of Mfd is only functional within the correct macromolecular context.
Autoinhibitory domains (AIDs)
Target domain |
49-985 (ATP-dependent DNA helicase); 467-545 (RNAP-interacting domain) |
Relief mechanism |
Partner binding |
Assay |
Deletion assay |
Accessory elements
No accessory elements
References
Autoinhibited structure

Activated structure

15 structures for P30958
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
2B2N | X-ray | 210 A | A/B | 1-333 | PDB |
2EYQ | X-ray | 320 A | A/B | 1-1148 | PDB |
3HJH | X-ray | 195 A | A | 1-470 | PDB |
4DFC | X-ray | 280 A | A/C | 127-213 | PDB |
6X26 | EM | 410 A | A | 1-1148 | PDB |
6X2F | EM | 400 A | A | 1-1148 | PDB |
6X2N | EM | 390 A | A | 1-1148 | PDB |
6X43 | EM | 360 A | A | 1-1148 | PDB |
6X4W | EM | 380 A | A | 1-1148 | PDB |
6X4Y | EM | 360 A | A | 1-1148 | PDB |
6X50 | EM | 330 A | A | 1-1148 | PDB |
6XEO | EM | 550 A | A | 1-1148 | PDB |
6YHZ | NMR | - | A | 472-547 | PDB |
7SSG | EM | 520 A | A | 1-1148 | PDB |
AF-P30958-F1 | Predicted | AlphaFoldDB |
No variants for P30958
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
No variants for P30958 |
No associated diseases with P30958
No regional properties for P30958
Type | Name | Position | InterPro Accession |
---|---|---|---|
No domain, repeats, and functional sites for P30958 |
Functions
Description | ||
---|---|---|
EC Number | ||
Subcellular Localization |
|
|
PANTHER Family | PTHR47964 | ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC |
PANTHER Subfamily | PTHR47964:SF1 | ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC |
PANTHER Protein Class | DNA metabolism protein | |
PANTHER Pathway Category | No pathway information available |
2 GO annotations of cellular component
Name | Definition |
---|---|
cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
DNA repair complex | A protein complex involved in DNA repair processes including direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway. |
6 GO annotations of molecular function
Name | Definition |
---|---|
ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
damaged DNA binding | Binding to damaged DNA. |
DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
DNA translocase activity | Generation of movement along a single- or double-stranded DNA molecule, driven by ATP hydrolysis. |
hydrolase activity | Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. |
RNA polymerase core enzyme binding | Binding to an RNA polymerase core enzyme, containing a specific subunit composition defined as the core enzyme. |
6 GO annotations of biological process
Name | Definition |
---|---|
DNA damage response | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism. |
DNA repair | The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway. |
nucleotide-excision repair, preincision complex assembly | The aggregation, arrangement and bonding together of proteins on DNA to form the multiprotein complex involved in damage recognition, DNA helix unwinding, and endonucleolytic cleavage at the site of DNA damage. This assembly occurs before the phosphodiester backbone of the damaged strand is cleaved 3' and 5' of the site of DNA damage. |
regulation of DNA-templated transcription | Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription. |
transcription-coupled nucleotide-excision repair | The nucleotide-excision repair process that carries out preferential repair of DNA lesions on the actively transcribed strand of the DNA duplex. In addition, the transcription-coupled nucleotide-excision repair pathway is required for the recognition and repair of a small subset of lesions that are not recognized by the global genome nucleotide excision repair pathway. |
transcription-coupled nucleotide-excision repair, DNA damage recognition | The identification of lesions on the actively transcribed strand of the DNA duplex as well as a small subset of lesions not recognized by the general nucleotide-excision repair pathway. |
No homologous proteins in AiPD
UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
---|---|---|---|---|
No homologous proteins |
10 | 20 | 30 | 40 | 50 | 60 |
MPEQYRYTLP | VKAGEQRLLG | ELTGAACATL | VAEIAERHAG | PVVLIAPDMQ | NALRLHDEIS |
70 | 80 | 90 | 100 | 110 | 120 |
QFTDQMVMNL | ADWETLPYDS | FSPHQDIISS | RLSTLYQLPT | MQRGVLIVPV | NTLMQRVCPH |
130 | 140 | 150 | 160 | 170 | 180 |
SFLHGHALVM | KKGQRLSRDA | LRTQLDSAGY | RHVDQVMEHG | EYATRGALLD | LFPMGSELPY |
190 | 200 | 210 | 220 | 230 | 240 |
RLDFFDDEID | SLRVFDVDSQ | RTLEEVEAIN | LLPAHEFPTD | KAAIELFRSQ | WRDTFEVKRD |
250 | 260 | 270 | 280 | 290 | 300 |
PEHIYQQVSK | GTLPAGIEYW | QPLFFSEPLP | PLFSYFPANT | LLVNTGDLET | SAERFQADTL |
310 | 320 | 330 | 340 | 350 | 360 |
ARFENRGVDP | MRPLLPPQSL | WLRVDELFSE | LKNWPRVQLK | TEHLPTKAAN | ANLGFQKLPD |
370 | 380 | 390 | 400 | 410 | 420 |
LAVQAQQKAP | LDALRKFLET | FDGPVVFSVE | SEGRREALGE | LLARIKIAPQ | RIMRLDEASD |
430 | 440 | 450 | 460 | 470 | 480 |
RGRYLMIGAA | EHGFVDTVRN | LALICESDLL | GERVARRRQD | SRRTINPDTL | IRNLAELHIG |
490 | 500 | 510 | 520 | 530 | 540 |
QPVVHLEHGV | GRYAGMTTLE | AGGITGEYLM | LTYANDAKLY | VPVSSLHLIS | RYAGGAEENA |
550 | 560 | 570 | 580 | 590 | 600 |
PLHKLGGDAW | SRARQKAAEK | VRDVAAELLD | IYAQRAAKEG | FAFKHDREQY | QLFCDSFPFE |
610 | 620 | 630 | 640 | 650 | 660 |
TTPDQAQAIN | AVLSDMCQPL | AMDRLVCGDV | GFGKTEVAMR | AAFLAVDNHK | QVAVLVPTTL |
670 | 680 | 690 | 700 | 710 | 720 |
LAQQHYDNFR | DRFANWPVRI | EMISRFRSAK | EQTQILAEVA | EGKIDILIGT | HKLLQSDVKF |
730 | 740 | 750 | 760 | 770 | 780 |
KDLGLLIVDE | EHRFGVRHKE | RIKAMRANVD | ILTLTATPIP | RTLNMAMSGM | RDLSIIATPP |
790 | 800 | 810 | 820 | 830 | 840 |
ARRLAVKTFV | REYDSMVVRE | AILREILRGG | QVYYLYNDVE | NIQKAAERLA | ELVPEARIAI |
850 | 860 | 870 | 880 | 890 | 900 |
GHGQMREREL | ERVMNDFHHQ | RFNVLVCTTI | IETGIDIPTA | NTIIIERADH | FGLAQLHQLR |
910 | 920 | 930 | 940 | 950 | 960 |
GRVGRSHHQA | YAWLLTPHPK | AMTTDAQKRL | EAIASLEDLG | AGFALATHDL | EIRGAGELLG |
970 | 980 | 990 | 1000 | 1010 | 1020 |
EEQSGSMETI | GFSLYMELLE | NAVDALKAGR | EPSLEDLTSQ | QTEVELRMPS | LLPDDFIPDV |
1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
NTRLSFYKRI | ASAKTENELE | EIKVELIDRF | GLLPDPARTL | LDIARLRQQA | QKLGIRKLEG |
1090 | 1100 | 1110 | 1120 | 1130 | 1140 |
NEKGGVIEFA | EKNHVNPAWL | IGLLQKQPQH | YRLDGPTRLK | FIQDLSERKT | RIEWVRQFMR |
ELEENAIA |