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Protein

Repressor protein c

Gene

repc

Organism
Enterobacteria phage Mu (Bacteriophage Mu)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Promotes latency by binding operators O1 and O2 in the enhancer/operator region, thereby repressing the transcription from the Pe (early) promoter and blocking the expression of the genes required for replication (lytic growth). Competes with DDE-recombinase A for binding to the internal activation sequence (IAS), which overlaps O1 and O2. The outcome of this competition determines if the virus enters latency or starts replication. Makes the cell immune to superinfection by repressing genes expression of any subsequent incoming viral genome.5 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Host-virus interaction, Latency-replication switch, Transcription, Transcription regulation, Viral latency

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Repressor protein c
Short name:
Repc
Alternative name(s):
CI
Gene product 1
Short name:
gp1
Mu repressor
Short name:
MuR
Gene namesi
Name:repc
Synonyms:c
Ordered Locus Names:Mup01
OrganismiEnterobacteria phage Mu (Bacteriophage Mu)
Taxonomic identifieri10677 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeMulikevirus
Virus hostiEnterobacteriaceae [TaxID: 543]
Proteomesi
  • UP000002611 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

  • host cell cytoplasm Source: UniProtKB-SubCell
  • transcriptional repressor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi183V → S: Resistant to ClpX-ClpP degradation. 1 Publication1
Mutagenesisi193K → S: Resistant to ClpX-ClpP degradation. 1 Publication1
Mutagenesisi196V → S: Resistant to ClpX-ClpP degradation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000775891 – 196Repressor protein cAdd BLAST196

Post-translational modificationi

C-terminally truncated forms act as exceptionally stable repressors that prevent prophage induction.

Expressioni

Inductioni

Expressed in the early phase of the viral replicative cycle. When present at high concentration, negatively regulates its own expression by binding to O3 (PcM promoter). PcM promoter, and thus Repc expression, is blocked by Ner. The host SsrA, the ClpXP host protease that degrades Repressor c protein, the Lon protease, and the stationary phase-specific sigma factor RpoS are all influencing Mu repression in response to either temperature or stationary growth phase. Decreased availability of host SsrA in growing cells would favor latency, whereas starvation would favor Repc degradation and hence induction.2 Publications

Keywords - Developmental stagei

Early protein

Interactioni

Subunit structurei

Homodimer. Three homodimers assemble as a homohexamer (Probable).1 Publication

Structurei

Secondary structure

1196
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi19 – 23Combined sources5
Helixi32 – 42Combined sources11
Beta strandi46 – 48Combined sources3
Turni53 – 56Combined sources4
Beta strandi58 – 60Combined sources3
Helixi62 – 64Combined sources3
Helixi67 – 77Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G4DNMR-A13-81[»]
1QPMNMR-A13-81[»]
SMRiP06019.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06019.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini13 – 81HTH Mu-typePROSITE-ProRule annotationAdd BLAST69

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni192 – 196Recognition by host ClpX-ClpP5

Domaini

The winged HTH N-terminal domain cooperatively binds to three operators O1, O2, and O3 with respectively 3, 4 and 2 binding sites. The C-terminal domain (CTD) regulates DNA binding by the N-terminal domain and degradation by ClpX-ClpP protease.1 Publication

Sequence similaritiesi

Contains 1 HTH Mu-type domain.Curated

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR009061. DNA-bd_dom_put.
IPR003314. Mu-type_HTH.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF02316. HTH_Tnp_Mu_1. 1 hit.
[Graphical view]
SUPFAMiSSF46955. SSF46955. 1 hit.
PROSITEiPS51702. HTH_MU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P06019-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSNFIEKNN TEKSIWCSPQ EIMAADGMPG SVAGVHYRAN VQGWTKQKKE
60 70 80 90 100
GVKGGKAVEY DVMSMPTKER EQVIAHLGLS TPDTGAQANE KQDSSELINK
110 120 130 140 150
LTTTLINMIE ELEPDEARKA LKLLSKGGLL ALMPLVFNEQ KLYSFIGFSQ
160 170 180 190
QSIQTLMMLD ALPEEKRKEI LSKYGIHEQE SVVVPSQEPQ EVKKAV
Length:196
Mass (Da):21,822
Last modified:May 14, 2014 - v2
Checksum:i11BFBDF143934E88
GO

Sequence cautioni

The sequence AAA32376 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAF01132 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA24711 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01464 Genomic DNA. Translation: CAA24711.1. Different initiation.
M64097 Genomic DNA. Translation: AAA32376.1. Different initiation.
AF083977 Genomic DNA. Translation: AAF01132.1. Different initiation.
PIRiS07291.
RefSeqiNP_050605.1. NC_000929.1.

Genome annotation databases

GeneIDi2636266.
KEGGivg:2636266.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01464 Genomic DNA. Translation: CAA24711.1. Different initiation.
M64097 Genomic DNA. Translation: AAA32376.1. Different initiation.
AF083977 Genomic DNA. Translation: AAF01132.1. Different initiation.
PIRiS07291.
RefSeqiNP_050605.1. NC_000929.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G4DNMR-A13-81[»]
1QPMNMR-A13-81[»]
SMRiP06019.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2636266.
KEGGivg:2636266.

Miscellaneous databases

EvolutionaryTraceiP06019.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR009061. DNA-bd_dom_put.
IPR003314. Mu-type_HTH.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF02316. HTH_Tnp_Mu_1. 1 hit.
[Graphical view]
SUPFAMiSSF46955. SSF46955. 1 hit.
PROSITEiPS51702. HTH_MU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiREPC_BPMU
AccessioniPrimary (citable) accession number: P06019
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: May 14, 2014
Last modified: November 2, 2016
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Caution

Translation initiates from a non-canonical start codon (UUG).Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.