| Tag | Content |
|---|
| CPLM ID | CPLM-005931 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Transcription-repair-coupling factor |
Protein Synonyms/Alias | TRCF; ATP-dependent helicase mfd |
Gene Name | mfd |
Gene Synonyms/Alias | b1114; JW1100 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 221 | AHEFPTDKAAIELFR | acetylation | [1] | | 238 | WRDTFEVKRDPEHIY | acetylation | [1] | | 332 | DELFSELKNWPRVQL | acetylation | [1] | | 347 | KTEHLPTKAANANLG | acetylation | [1] | | 357 | NANLGFQKLPDLAVQ | acetylation | [1] | | 544 | EENAPLHKLGGDAWS | acetylation | [1] | | 712 | DILIGTHKLLQSDVK | acetylation | [1, 2] | | 719 | KLLQSDVKFKDLGLL | acetylation | [1] | | 721 | LQSDVKFKDLGLLIV | acetylation | [1] | | 824 | NDVENIQKAAERLAE | acetylation | [1] | | 1034 | YKRIASAKTENELEE | acetylation | [1] | | 1043 | ENELEEIKVELIDRF | acetylation | [1] | | 1083 | RKLEGNEKGGVIEFA | acetylation | [1] | | 1092 | GVIEFAEKNHVNPAW | acetylation | [1] | | 1106 | WLIGLLQKQPQHYRL | acetylation | [1] | | 1120 | LDGPTRLKFIQDLSE | acetylation | [1] |
|
Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli. Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z. J Proteome Res. 2013 Feb 1;12(2):844-51. [ PMID: 23294111] |
Functional Description | Necessary for strand-specific repair. A lesion in the template strand blocks the RNA polymerase complex (RNAP). The RNAP-DNA-RNA complex is specifically recognized by TRCF which releases RNAP and the truncated transcript; the TCRF may replace RNAP at the lesion site and then recruit the UvrA/B/C repair system. |
Sequence Annotation | DOMAIN 615 776 Helicase ATP-binding.
DOMAIN 798 951 Helicase C-terminal.
NP_BIND 628 635 ATP (Potential).
MOTIF 729 732 DEEH box. |
Keyword | 3D-structure; ATP-binding; Complete proteome; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1148 AA |
Protein Sequence | MPEQYRYTLP VKAGEQRLLG ELTGAACATL VAEIAERHAG PVVLIAPDMQ NALRLHDEIS 60
QFTDQMVMNL ADWETLPYDS FSPHQDIISS RLSTLYQLPT MQRGVLIVPV NTLMQRVCPH 120
SFLHGHALVM KKGQRLSRDA LRTQLDSAGY RHVDQVMEHG EYATRGALLD LFPMGSELPY 180
RLDFFDDEID SLRVFDVDSQ RTLEEVEAIN LLPAHEFPTD KAAIELFRSQ WRDTFEVKRD 240
PEHIYQQVSK GTLPAGIEYW QPLFFSEPLP PLFSYFPANT LLVNTGDLET SAERFQADTL 300
ARFENRGVDP MRPLLPPQSL WLRVDELFSE LKNWPRVQLK TEHLPTKAAN ANLGFQKLPD 360
LAVQAQQKAP LDALRKFLET FDGPVVFSVE SEGRREALGE LLARIKIAPQ RIMRLDEASD 420
RGRYLMIGAA EHGFVDTVRN LALICESDLL GERVARRRQD SRRTINPDTL IRNLAELHIG 480
QPVVHLEHGV GRYAGMTTLE AGGITGEYLM LTYANDAKLY VPVSSLHLIS RYAGGAEENA 540
PLHKLGGDAW SRARQKAAEK VRDVAAELLD IYAQRAAKEG FAFKHDREQY QLFCDSFPFE 600
TTPDQAQAIN AVLSDMCQPL AMDRLVCGDV GFGKTEVAMR AAFLAVDNHK QVAVLVPTTL 660
LAQQHYDNFR DRFANWPVRI EMISRFRSAK EQTQILAEVA EGKIDILIGT HKLLQSDVKF 720
KDLGLLIVDE EHRFGVRHKE RIKAMRANVD ILTLTATPIP RTLNMAMSGM RDLSIIATPP 780
ARRLAVKTFV REYDSMVVRE AILREILRGG QVYYLYNDVE NIQKAAERLA ELVPEARIAI 840
GHGQMREREL ERVMNDFHHQ RFNVLVCTTI IETGIDIPTA NTIIIERADH FGLAQLHQLR 900
GRVGRSHHQA YAWLLTPHPK AMTTDAQKRL EAIASLEDLG AGFALATHDL EIRGAGELLG 960
EEQSGSMETI GFSLYMELLE NAVDALKAGR EPSLEDLTSQ QTEVELRMPS LLPDDFIPDV 1020
NTRLSFYKRI ASAKTENELE EIKVELIDRF GLLPDPARTL LDIARLRQQA QKLGIRKLEG 1080
NEKGGVIEFA EKNHVNPAWL IGLLQKQPQH YRLDGPTRLK FIQDLSERKT RIEWVRQFMR 1140
ELEENAIA 1148 |
Gene Ontology | GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0008026; F:ATP-dependent helicase activity; IDA:EcoCyc. GO:0003684; F:damaged DNA binding; IEA:InterPro. GO:0003677; F:DNA binding; IDA:EcoCyc. GO:0006355; P:regulation of transcription, DNA-dependent; IDA:EcoliWiki. GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IDA:EcoCyc. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |