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Protein

Transcription termination/antitermination protein NusA

Gene

nusA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Participates in both transcription termination and antitermination. Involved in a variety of cellular and viral termination and antitermination processes, such as Rho-dependent transcriptional termination, intrinsic termination, and phage lambda N-mediated transcriptional antitermination. Also important for coordinating the cellular responses to DNA damage by coupling the processes of nucleotide excision repair and translesion synthesis to transcription.UniRule annotation9 Publications

GO - Molecular functioni

  • bacterial-type RNA polymerase core enzyme binding Source: CAFA
  • DNA binding transcription factor activity Source: InterPro
  • nucleotide binding Source: InterPro
  • protein domain specific binding Source: CAFA
  • RNA binding Source: UniProtKB-KW

GO - Biological processi

  • transcription antitermination Source: EcoliWiki
  • transcription termination from bacterial-type RNA polymerase promoter Source: CAFA

Keywordsi

Molecular functionRNA-binding
Biological processStress response, Transcription, Transcription antitermination, Transcription regulation, Transcription termination

Enzyme and pathway databases

BioCyciEcoCyc:EG10665-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription termination/antitermination protein NusAUniRule annotation
Alternative name(s):
N utilization substance protein A
Transcription termination/antitermination L factor
Gene namesi
Name:nusAUniRule annotation
Ordered Locus Names:b3169, JW3138
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10665 nusA

Subcellular locationi

  • Cytoplasm UniRule annotation1 Publication
  • Note: Colocalizes with nucleoids.

GO - Cellular componenti

  • cytosol Source: EcoCyc

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Mutants are sensitive to DNA-damaging agents.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi104R → H in nusA10-1. 1 Publication1
Mutagenesisi181G → D in nusa11; inability to terminate transcription normally at termination sites. 1 Publication1
Mutagenesisi183L → R in nusA1; restricts lambda growth by preventing antitermination activity of lambda N protein. 1 Publication1
Mutagenesisi212E → K in nusA10-2. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001819651 – 495Transcription termination/antitermination protein NusAAdd BLAST495

Proteomic databases

EPDiP0AFF6
PaxDbiP0AFF6
PRIDEiP0AFF6

2D gel databases

SWISS-2DPAGEiP0AFF6

Expressioni

Inductioni

In response to low temperature. Negatively autoregulated. Induced by cold shock (42 to 15 degrees Celsius) (at protein level) (PubMed:8898389).3 Publications

Interactioni

Subunit structurei

Monomer. Binds directly to the core enzyme of the DNA-dependent RNA polymerase and to nascent RNA. Also interacts with the termination Rho factor and the phage lambda N protein.UniRule annotation5 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • bacterial-type RNA polymerase core enzyme binding Source: CAFA
  • protein domain specific binding Source: CAFA

Protein-protein interaction databases

BioGridi4261878, 15 interactors
DIPiDIP-47857N
IntActiP0AFF6, 45 interactors
STRINGi316385.ECDH10B_3343

Structurei

Secondary structure

1495
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 16Combined sources14
Helixi20 – 39Combined sources20
Beta strandi45 – 50Combined sources6
Turni51 – 54Combined sources4
Beta strandi55 – 65Combined sources11
Turni71 – 73Combined sources3
Beta strandi74 – 76Combined sources3
Helixi77 – 84Combined sources8
Beta strandi92 – 96Combined sources5
Helixi102 – 104Combined sources3
Helixi110 – 132Combined sources23
Turni133 – 135Combined sources3
Beta strandi136 – 145Combined sources10
Beta strandi147 – 153Combined sources7
Beta strandi159 – 163Combined sources5
Helixi164 – 166Combined sources3
Beta strandi178 – 186Combined sources9
Beta strandi195 – 201Combined sources7
Helixi202 – 212Combined sources11
Helixi214 – 217Combined sources4
Beta strandi220 – 229Combined sources10
Turni230 – 232Combined sources3
Beta strandi233 – 240Combined sources8
Helixi247 – 252Combined sources6
Helixi254 – 256Combined sources3
Helixi257 – 265Combined sources9
Turni266 – 268Combined sources3
Beta strandi270 – 275Combined sources6
Helixi280 – 287Combined sources8
Turni288 – 290Combined sources3
Beta strandi293 – 299Combined sources7
Turni300 – 303Combined sources4
Beta strandi304 – 309Combined sources6
Helixi314 – 318Combined sources5
Helixi320 – 322Combined sources3
Helixi323 – 332Combined sources10
Beta strandi335 – 340Combined sources6
Helixi354 – 363Combined sources10
Helixi367 – 375Combined sources9
Helixi381 – 386Combined sources6
Helixi389 – 392Combined sources4
Turni395 – 397Combined sources3
Helixi400 – 417Combined sources18
Helixi432 – 435Combined sources4
Helixi442 – 449Combined sources8
Turni450 – 452Combined sources3
Helixi456 – 460Combined sources5
Helixi464 – 468Combined sources5
Beta strandi470 – 472Combined sources3
Helixi475 – 489Combined sources15
Turni491 – 493Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U9LX-ray1.90A/B352-421[»]
1WCLNMR-A351-426[»]
1WCNNMR-A426-495[»]
2JZBNMR-B424-495[»]
2KWPNMR-A1-125[»]
5LM9X-ray2.14A101-426[»]
5MS0electron microscopy9.80M1-495[»]
6FLQelectron microscopy4.10F1-495[»]
ProteinModelPortaliP0AFF6
SMRiP0AFF6
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AFF6

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini135 – 200S1 motifUniRule annotationAdd BLAST66
Domaini230 – 293KH 1UniRule annotationAdd BLAST64
Domaini302 – 368KH 2UniRule annotationAdd BLAST67
Repeati364 – 4141Add BLAST51
Repeati439 – 4892Add BLAST51

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni364 – 4892 X 51 AA approximate repeatsAdd BLAST126

Domaini

The N-terminal region interacts with RNA polymerase. The central region is composed of 3 RNA binding domains, S1, KH 1 and KH 2. The C-terminal region contains 2 acidic repeats, AR1 and AR2, which bind to protein N from phage lambda during antitermination.3 Publications

Sequence similaritiesi

Belongs to the NusA family.UniRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105CHV Bacteria
COG0195 LUCA
HOGENOMiHOG000006394
InParanoidiP0AFF6
KOiK02600
OMAiSRTTPKM
PhylomeDBiP0AFF6

Family and domain databases

Gene3Di3.30.1480.10, 1 hit
3.30.300.20, 2 hits
HAMAPiMF_00945_B NusA_B, 1 hit
InterProiView protein in InterPro
IPR010995 DNA_repair_Rad51/TF_NusA_a-hlx
IPR015946 KH_dom-like_a/b
IPR025249 KH_dom_NusA-like
IPR009019 KH_sf_prok-type
IPR012340 NA-bd_OB-fold
IPR030842 NusA_bac
IPR036555 NusA_N_sf
IPR022967 S1_dom
IPR003029 S1_domain
IPR013735 TF_NusA_N
IPR010214 Tscrpt_termin_fac_NusA_C_rpt
IPR010213 Tscrpt_termination_fac_NusA
PfamiView protein in Pfam
PF13184 KH_5, 1 hit
PF08529 NusA_N, 1 hit
PF00575 S1, 1 hit
SMARTiView protein in SMART
SM00316 S1, 1 hit
SUPFAMiSSF47794 SSF47794, 2 hits
SSF50249 SSF50249, 1 hit
SSF54814 SSF54814, 2 hits
SSF69705 SSF69705, 1 hit
TIGRFAMsiTIGR01953 NusA, 1 hit
TIGR01954 nusA_Cterm_rpt, 2 hits
PROSITEiView protein in PROSITE
PS50084 KH_TYPE_1, 1 hit
PS50126 S1, 1 hit

Sequencei

Sequence statusi: Complete.

P0AFF6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKEILAVVE AVSNEKALPR EKIFEALESA LATATKKKYE QEIDVRVQID
60 70 80 90 100
RKSGDFDTFR RWLVVDEVTQ PTKEITLEAA RYEDESLNLG DYVEDQIESV
110 120 130 140 150
TFDRITTQTA KQVIVQKVRE AERAMVVDQF REHEGEIITG VVKKVNRDNI
160 170 180 190 200
SLDLGNNAEA VILREDMLPR ENFRPGDRVR GVLYSVRPEA RGAQLFVTRS
210 220 230 240 250
KPEMLIELFR IEVPEIGEEV IEIKAAARDP GSRAKIAVKT NDKRIDPVGA
260 270 280 290 300
CVGMRGARVQ AVSTELGGER IDIVLWDDNP AQFVINAMAP ADVASIVVDE
310 320 330 340 350
DKHTMDIAVE AGNLAQAIGR NGQNVRLASQ LSGWELNVMT VDDLQAKHQA
360 370 380 390 400
EAHAAIDTFT KYLDIDEDFA TVLVEEGFST LEELAYVPMK ELLEIEGLDE
410 420 430 440 450
PTVEALRERA KNALATIAQA QEESLGDNKP ADDLLNLEGV DRDLAFKLAA
460 470 480 490
RGVCTLEDLA EQGIDDLADI EGLTDEKAGA LIMAARNICW FGDEA
Length:495
Mass (Da):54,871
Last modified:December 20, 2005 - v1
Checksum:i7D4DD019172FBAD0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti167 – 191MLPRE…RPEAR → SCRVKTFALATAFVACSIPF ARNG in CAA25200 (PubMed:6326058).CuratedAdd BLAST25

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00513 Genomic DNA Translation: CAA25200.1
U18997 Genomic DNA Translation: AAA57972.1
U00096 Genomic DNA Translation: AAC76203.1
AP009048 Genomic DNA Translation: BAE77215.1
PIRiE65107 FJEC
RefSeqiNP_417638.1, NC_000913.3
WP_001031057.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76203; AAC76203; b3169
BAE77215; BAE77215; BAE77215
GeneIDi947682
KEGGiecj:JW3138
eco:b3169
PATRICifig|1411691.4.peg.3561

Similar proteinsi

Entry informationi

Entry nameiNUSA_ECOLI
AccessioniPrimary (citable) accession number: P0AFF6
Secondary accession number(s): P03003, Q2M941
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 20, 2005
Last modified: May 23, 2018
This is version 117 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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