Respiratory nitrate reductase 2 gamma chain

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P0AF33 (NARV_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 52. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Recommended name:
Respiratory nitrate reductase 2 gamma chain
EC=1.7.99.4

Gene names

Name:	narV
Ordered Locus Names:	Z2247, ECs2068

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	226 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	This is a second nitrate reductase enzyme which can substitute for the NRA enzyme and allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The gamma chain is a membrane-embedded heme-iron unit resembling cytochrome b, which transfers electrons from quinones to the beta subunit By similarity.
Catalytic activity	Nitrite + acceptor = nitrate + reduced acceptor.
Cofactor	Binds 2 heme groups per subunit. Heme 1 is located at the cytoplasmic interface, heme 2 is located at the periplasmic interface. Electrons are transferred from the periplasmic to the cytoplasmic heme By similarity.
Subunit structure	Dimer of heterotrimers each composed of an alpha, a beta and a gamma chain. Alpha and beta are catalytic chains; gamma chains are involved in binding the enzyme complex to the cytoplasmic membrane By similarity.
Subcellular location	Cell inner membrane; Multi-pass membrane protein By similarity.

Ontologies

Keywords
Biological process	Electron transport Nitrate assimilation Transport
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW nitrate assimilation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nitrate reductase complex Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nitrate reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 226

226

Respiratory nitrate reductase 2 gamma chain

PRO_0000096732

Regions

Topological domain

2 – 4

Periplasmic By similarity

Transmembrane

5 – 30

Helical; Name=1; By similarity

Topological domain

31 – 48

Cytoplasmic By similarity

Transmembrane

49 – 71

Helical; Name=2; By similarity

Topological domain

72 – 83

Periplasmic By similarity

Transmembrane

84 – 113

Helical; Name=3; By similarity

Topological domain

114 – 125

Cytoplasmic By similarity

Transmembrane

126 – 149

Helical; Name=4; By similarity

Topological domain

150 – 183

Periplasmic By similarity

Transmembrane

184 – 199

Helical; Name=5; By similarity

Topological domain

200 – 226

Cytoplasmic By similarity

Sites

Metal binding

Iron (heme B 1 axial ligand) By similarity

Metal binding

Iron (heme B 2 axial ligand) By similarity

Metal binding

188

Iron (heme B 2 axial ligand) By similarity

Metal binding

206

Iron (heme B 1 axial ligand) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P0AF33 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 1D5FAC307F3D5B84
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FASTA

226

26,018

        10         20         30         40         50         60 
MIQYLNVFFY DIYPYICATV FFLGSWLRYD YGQYTWRASS SQMLDKRGMV IWSNLFHIGI 

        70         80         90        100        110        120 
LGIFFGHLFG MLTPHWMYAW FLPVAAKQLM AMVLGGICGV LTLIGGAGLL WRRLTNQRVR 

       130        140        150        160        170        180 
ATSTTPDIII MSILLIQCLL GLSTIPFSAQ YPDGSEMMKL VGWAQSIVTF RGGSSEMLNG 

       190        200        210        220 
VAFVFRLHLV LGMTIFLLFP FTRLVHVWSA PFEYFTRRYQ IVRSRR

« Hide

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W.

Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.

Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG56305.1. BA000007 Genomic DNA. Translation: BAB35491.1.
PIR	D90887. E85730.
RefSeq	NP_287691.1. NC_002655.2. NP_310095.1. NC_002695.1.
3D structure databases
ProteinModelPortal	P0AF33.
SMR	P0AF33. Positions 3-225.
ModBase	Search...
Protein-protein interaction databases
STRING	155864.Z2247.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAG56305; AAG56305; Z2247. BAB35491; BAB35491; BAB35491.
GeneID	917268. 960731.
KEGG	ece:Z2247. ecs:ECs2068.
PATRIC	18353209. VBIEscCol44059_1824.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG2181.
HOGENOM	HOG000237376.
KO	K08347.
OMA	LTPHWVY.
ProtClustDB	CLSK880007.
Enzyme and pathway databases
BioCyc	ECOL386585:GJFA-2040-MONOMER.
Family and domain databases
InterPro	IPR023234. NarG-like_domain. IPR003816. Nitrate_red_gam. [Graphical view]
Pfam	PF02665. Nitrate_red_gam. 1 hit. [Graphical view]
SUPFAM	SSF103501. NarG-like_domain. 1 hit.
TIGRFAMs	TIGR00351. narI. 1 hit.
ProtoNet	Search...

Entry information

Entry name

NARV_ECO57

Accession

Primary (citable) accession number: P0AF33
Secondary accession number(s): P19316

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	May 1, 2013
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information