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P0A9X1 (ZNUC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Zinc import ATP-binding protein ZnuC

EC=3.6.3.-
Gene names
Name:znuC
Synonyms:yebM
Ordered Locus Names:b1858, JW1847
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length251 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. Ref.5

Enzyme regulation

Inhibited by arsenate. Ref.5

Subunit structure

The complex is composed of two ATP-binding proteins (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA) Potential.

Subcellular location

Cell inner membrane; Peripheral membrane protein By similarity.

Induction

Transcriptionally repressed by zur (zinc uptake regulator), in response to high extracellular zinc concentrations. Ref.5 Ref.6

Sequence similarities

Belongs to the ABC transporter superfamily. Zinc importer (TC 3.A.1.15.5) family. [View classification]

Contains 1 ABC transporter domain.

Sequence caution

The sequence U38702 differs from that shown. Reason: Frameshift at position 188.

Ontologies

Keywords
   Biological processIon transport
Transport
Zinc transport
   Cellular componentCell inner membrane
Cell membrane
Membrane
   LigandATP-binding
Nucleotide-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from electronic annotation. Source: GOC

   Cellular_componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from electronic annotation. Source: InterPro

zinc transporting ATPase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 251251Zinc import ATP-binding protein ZnuC
PRO_0000093130

Regions

Domain5 – 220216ABC transporter
Nucleotide binding37 – 448ATP Potential

Experimental info

Sequence conflict80 – 834TTLP → STLS in U38702. Ref.1
Sequence conflict1351L → W in U38702. Ref.1
Sequence conflict1431V → A in U38702. Ref.1
Sequence conflict1551G → W in U38702. Ref.1
Sequence conflict174 – 1763VLM → ALL in U38702. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P0A9X1 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: F4BF845AC3C7904C

FASTA25127,867
        10         20         30         40         50         60 
MTSLVSLENV SVSFGQRRVL SDVSLELKPG KILTLLGPNG AGKSTLVRVV LGLVTPDEGV 

        70         80         90        100        110        120 
IKRNGKLRIG YVPQKLYLDT TLPLTVNRFL RLRPGTHKED ILPALKRVQA GHLINAPMQK 

       130        140        150        160        170        180 
LSGGETQRVL LARALLNRPQ LLVLDEPTQG VDVNGQVALY DLIDQLRREL DCGVLMVSHD 

       190        200        210        220        230        240 
LHLVMAKTDE VLCLNHHICC SGTPEVVSLH PEFISMFGPR GAEQLGIYRH HHNHRHDLQG 

       250 
RIVLRRGNDR S 

« Hide

References

« Hide 'large scale' references
[1]Robison K., O'Keeffe T., Church G.M.
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / EMG2.
[2]"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. expand/collapse author list , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli."
Patzer S.I., Hantke K.
Mol. Microbiol. 28:1199-1210(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ZINC TRANSPORT, INDUCTION, ATPASE ACTIVITY, ENZYME REGULATION.
Strain: K12.
[6]"Transcriptional response of Escherichia coli to external zinc."
Yamamoto K., Ishihama A.
J. Bacteriol. 187:6333-6340(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U38702 Genomic DNA. No translation available.
U00096 Genomic DNA. Translation: AAC74928.1.
AP009048 Genomic DNA. Translation: BAA15666.1.
PIRB64948.
RefSeqNP_416372.1. NC_000913.2.
YP_490120.1. NC_007779.1.

3D structure databases

ProteinModelPortalP0A9X1.
SMRP0A9X1. Positions 5-230.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-48234N.
IntActP0A9X1. 13 interactions.
STRING511145.b1858.

Protein family/group databases

TCDB3.A.1.15.5. ATP-binding cassette (ABC) superfamily.

Proteomic databases

PaxDbP0A9X1.
PRIDEP0A9X1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74928; AAC74928; b1858.
BAA15666; BAA15666; BAA15666.
GeneID12934230.
946374.
KEGGecj:Y75_p1834.
eco:b1858.
PATRIC32119039. VBIEscCol129921_1937.

Organism-specific databases

EchoBASEEB2931.
EcoGeneEG13132. znuC.

Phylogenomic databases

eggNOGCOG1121.
KOK09817.
OMALCLNQHV.
ProtClustDBPRK09544.

Enzyme and pathway databases

BioCycEcoCyc:ZNUC-MONOMER.
ECOL316407:JW1847-MONOMER.

Gene expression databases

GenevestigatorP0A9X1.

Family and domain databases

InterProIPR003593. AAA+_ATPase.
IPR003439. ABC_transporter-like.
IPR017882. ABC_transptr_Zn_ATP-bd_ZnuC.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00005. ABC_tran. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00211. ABC_TRANSPORTER_1. False negative.
PS50893. ABC_TRANSPORTER_2. 1 hit.
PS51298. ZNUC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameZNUC_ECOLI
AccessionPrimary (citable) accession number: P0A9X1
Secondary accession number(s): P52648, P76285
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: May 29, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families