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Escherichia coli K-12 substr. MG1655 Polypeptide: Zn2+ ABC transporter - membrane subunit



Gene: znuB Accession Numbers: EG12368 (EcoCyc), b1859, ECK1860

Synonyms: yebI

Regulation Summary Diagram: ?

Component of: Zn2+ ABC transporter (extended summary available)

Summary:
membrane component of ABC transporter

Gene Citations: [Patzer98]

Locations: inner membrane

Map Position: [1,941,438 -> 1,942,223] (41.84 centisomes)
Length: 786 bp / 261 aa

Molecular Weight of Polypeptide: 27.729 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0006201 , EchoBASE:EB2271 , EcoGene:EG12368 , EcoliWiki:b1859 , ModBase:P39832 , OU-Microarray:b1859 , PortEco:znuB , PR:PRO_000024253 , Protein Model Portal:P39832 , RefSeq:NP_416373 , RegulonDB:EG12368 , String:511145.b1859 , UniProt:P39832

Relationship Links: InterPro:IN-FAMILY:IPR001626 , Pfam:IN-FAMILY:PF00950

In Paralogous Gene Group: 260 (2 members)

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006810 - transport Inferred by computational analysis [UniProtGOA11]
GO:0006811 - ion transport Inferred by computational analysis [UniProtGOA11]
GO:0006829 - zinc ion transport Inferred by computational analysis [UniProtGOA11]
GO:0055085 - transmembrane transport Inferred by computational analysis [GOA01]
Molecular Function: GO:0005524 - ATP binding Inferred by computational analysis [GOA01]
GO:0042626 - ATPase activity, coupled to transmembrane movement of substances Inferred by computational analysis [GOA01]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, DiazMejia09, Daley05]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11]

MultiFun Terms: cell structure membrane
transport Channel-type Transporters Pyrophosphate Bond (ATP; GTP; P2) Hydrolysis-driven Active Transporters The ATP-binding Cassette (ABC) Superfamily + ABC-type Uptake Permeases ABC superfamily, membrane component

Essentiality data for znuB knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Subunit of: Zn2+ ABC transporter

Subunit composition of Zn2+ ABC transporter = [ZnuC]2[ZnuB]2[ZnuA]
         Zn2+ ABC transporter - ATP binding subunit = ZnuC (summary available)
         Zn2+ ABC transporter - membrane subunit = ZnuB (summary available)
         Zn2+ ABC transporter - periplasmic binding protein = ZnuA (summary available)

Summary:
ZnuABC is a high-affinity zinc uptake system that is a member of the ATP Binding Cassette (ABC) Superfamily [Wu95]. znuA encodes the periplasmic zinc-binding component of the transporter, while znuB encodes the membrane component, and znuC encodes the ATPase subunit. Complementation analysis of znu mutants showed that transport of zinc (II) ion was restored in the presence of znuABC cloned on a low-copy-number vector [Patzer98]. The three components of ZnuABC also show high nucleotide sequence similarity to the corresponding components of the AdcABC zinc transporter of S. pneumoniae as well as subunits of other ABC metal ion transporters. The high-affinity transport of zinc ion by ZnuABC is inhibited by arsenate, suggesting that ZnuABC-mediated transport is energized by ATP hydrolysis [Patzer98]. Analysis of LacZ fusions indicated that expression of znuA and znuB was regulated by the protein Zur, which has amino acid sequence similarity to the iron regulator Fur [Patzer98]. znuA and znuBC are transcribed divergently [Patzer98].

Locations: inner membrane

GO Terms:

Biological Process: GO:0071577 - zinc ion transmembrane transport Inferred from experiment [Patzer98]
Molecular Function: GO:0015633 - zinc transporting ATPase activity Inferred from experiment [Patzer98]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment [Patzer98]


Enzymatic reaction of: Zn2+ ABC transporter


Sequence Features

Feature Class Location Citations Comment
Transmembrane-Region 8 -> 28
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 54 -> 74
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 84 -> 104
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 122 -> 142
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 178 -> 198
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 214 -> 234
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 236 -> 256
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b1859 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG12368; confirmed by SwissProt match.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Daley05: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308(5726);1321-3. PMID: 15919996

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Patzer98: Patzer SI, Hantke K (1998). "The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli." Mol Microbiol 1998;28(6);1199-210. PMID: 9680209

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

Wu95: Wu LF, Mandrand-Berthelot MA (1995). "A family of homologous substrate-binding proteins with a broad range of substrate specificity and dissimilar biological functions." Biochimie 1995;77(9);744-50. PMID: 8789466

Other References Related to Gene Regulation

Outten01: Outten CE, O'Halloran TV (2001). "Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis." Science 292(5526);2488-92. PMID: 11397910

Patzer00: Patzer SI, Hantke K (2000). "The zinc-responsive regulator Zur and its control of the znu gene cluster encoding the ZnuABC zinc uptake system in Escherichia coli." J Biol Chem 275(32);24321-32. PMID: 10816566

Warner12: Warner DM, Levy SB (2012). "SoxS increases the expression of the zinc uptake system ZnuACB in an Escherichia coli murine pyelonephritis model." J Bacteriol 194(5);1177-85. PMID: 22210763

Yamamoto05b: Yamamoto K, Ishihama A (2005). "Transcriptional response of Escherichia coli to external zinc." J Bacteriol 187(18);6333-40. PMID: 16159766


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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