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



Gene: znuC Accession Numbers: G7018 (EcoCyc), b1858, ECK1859

Synonyms: yebM

Regulation Summary Diagram: ?

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

Summary:
ATP-binding component of ABC transporter

znuC is one of a network of genes believed to play a role in promoting the stress-induced mutagenesis (SIM) response of E. coli K-12 [Al12].

Gene Citations: [Patzer98]

Locations: inner membrane, cytosol

Map Position: [1,940,686 -> 1,941,441] (41.83 centisomes)
Length: 756 bp / 251 aa

Molecular Weight of Polypeptide: 27.867 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0006198 , DIP:DIP-48234N , EchoBASE:EB2931 , EcoGene:EG13132 , EcoliWiki:b1858 , ModBase:P0A9X1 , OU-Microarray:b1858 , PortEco:znuC , PR:PRO_000024254 , Pride:P0A9X1 , Protein Model Portal:P0A9X1 , RefSeq:NP_416372 , RegulonDB:G7018 , SMR:P0A9X1 , String:511145.b1858 , UniProt:P0A9X1

Relationship Links: InterPro:IN-FAMILY:IPR003439 , InterPro:IN-FAMILY:IPR003593 , InterPro:IN-FAMILY:IPR017882 , InterPro:IN-FAMILY:IPR027417 , Pfam:IN-FAMILY:PF00005 , Prosite:IN-FAMILY:PS00211 , Prosite:IN-FAMILY:PS50893 , Prosite:IN-FAMILY:PS51298 , Smart:IN-FAMILY:SM00382

In Paralogous Gene Group: 23 (75 members)

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006200 - ATP catabolic process Inferred by computational analysis [GOA01a]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0006811 - ion transport Inferred by computational analysis [UniProtGOA11a]
GO:0006829 - zinc ion transport Inferred by computational analysis [UniProtGOA11a]
GO:0008152 - metabolic process Inferred by computational analysis [UniProtGOA11a]
GO:0071577 - zinc ion transmembrane transport Inferred by computational analysis [GOA06, GOA01a]
Molecular Function: GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
GO:0015633 - zinc transporting ATPase activity Inferred by computational analysis [GOA06, GOA01a]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016887 - ATPase activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005829 - cytosol
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA01a]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]
GO:0043190 - ATP-binding cassette (ABC) transporter complex Inferred by computational analysis [GOA06]

MultiFun Terms: metabolism biosynthesis of building blocks cofactors, small molecule carriers heme, porphyrine
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 ATP binding cytoplasmic component

Essentiality data for znuC 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
Conserved-Region 5 -> 220
[UniProt09]
UniProt: ABC transporter;
Nucleotide-Phosphate-Binding-Region 37 -> 44
[UniProt10a]
UniProt: ATP; Non-Experimental Qualifier: potential;
Sequence-Conflict 80 -> 83
[Robison95, UniProt10]
Alternate sequence: TTLP → STLS; UniProt: (in Ref. 1; U38702);
Sequence-Conflict 135
[Robison95, UniProt10]
Alternate sequence: L → W; UniProt: (in Ref. 1; U38702);
Sequence-Conflict 143
[Robison95, UniProt10]
Alternate sequence: V → A; UniProt: (in Ref. 1; U38702);
Sequence-Conflict 155
[Robison95, UniProt10]
Alternate sequence: G → W; UniProt: (in Ref. 1; U38702);
Sequence-Conflict 174 -> 176
[Robison95, UniProt10]
Alternate sequence: VLM → ALL; UniProt: (in Ref. 1; U38702);


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


References

Al12: Al Mamun AA, Lombardo MJ, Shee C, Lisewski AM, Gonzalez C, Lin D, Nehring RB, Saint-Ruf C, Gibson JL, Frisch RL, Lichtarge O, Hastings PJ, Rosenberg SM (2012). "Identity and function of a large gene network underlying mutagenic repair of DNA breaks." Science 338(6112);1344-8. PMID: 23224554

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

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

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

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

Robison95: Robison K., Estep P., O'Keeffe T., Church G.M. (1995). Data submission to EMBL/GenBank/DDBJ databases on 1995-10.

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt10a: 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 the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords 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

Yamamoto05a: 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
Page generated by SRI International Pathway Tools version 18.5 on Mon Dec 22, 2014, biocyc11.