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Reviewed, UniProtKB/Swiss-Prot P0AB69 (PNTB_ECO57)

Last modified June 16, 2009. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    NAD(P) transhydrogenase subunit beta
    EC=1.6.1.2
Alternative name(s):
    Nicotinamide nucleotide transhydrogenase subunit beta
    Pyridine nucleotide transhydrogenase subunit beta
Gene names
Name: pntB
Ordered Locus Names: Z2597, ECs2308
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane By similarity.

Catalytic activity

NADPH + NAD+ = NADP+ + NADH.

Subunit structure

Heterodimer of an alpha and a beta chain By similarity.

Subcellular location

Cell inner membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the PNT beta subunit family.

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Ontologies

Keywords
   Cellular componentCell inner membrane
Cell membrane
Membrane
   DomainTransmembrane
   LigandNAD
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNAD(P)+ transhydrogenase (AB-specific) activity

Inferred from electronic annotation. Source: EC

NADP or NADPH binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 462462NAD(P) transhydrogenase subunit beta
PRO_0000199024

Regions

Topological domain1 – 33Periplasmic Potential
Transmembrane4 – 2421 Potential
Topological domain25 – 4521Cytoplasmic Potential
Transmembrane46 – 6621 Potential
Topological domain67 – 8216Periplasmic Potential
Transmembrane83 – 10321 Potential
Topological domain104 – 11512Cytoplasmic Potential
Transmembrane116 – 13621 Potential
Topological domain137 – 16428Periplasmic Potential
Transmembrane165 – 18521 Potential
Topological domain186 – 1883Cytoplasmic Potential
Transmembrane189 – 20921 Potential
Topological domain210 – 2156Periplasmic Potential
Transmembrane216 – 23621 Potential
Topological domain237 – 2393Cytoplasmic Potential
Transmembrane240 – 26021 Potential
Topological domain261 – 30848Periplasmic Potential
Transmembrane309 – 32921 Potential
Topological domain330 – 462133Cytoplasmic Potential

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Sequences

Sequence LengthMass (Da)Tools
P0AB69-1 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: D11747291D271A2F

FASTA46248,723
        10         20         30         40         50         60 
MSGGLVTAAY IVAAILFIFS LAGLSKHETS RQGNNFGIAG MAIALIATIF GPDTGNVGWI 

        70         80         90        100        110        120 
LLAMVIGGAI GIRLAKKVEM TEMPELVAIL HSFVGLAAVL VGFNSYLHHD AGMAPILVNI 

       130        140        150        160        170        180 
HLTEVFLGIF IGAVTFTGSV VAFGKLCGKI SSKPLMLPNR HKMNLAALVV SFLLLIVFVR 

       190        200        210        220        230        240 
TDSVGLQVLA LLIMTAIALV FGWHLVASIG GADMPVVVSM LNSYSGWAAA AAGFMLSNDL 

       250        260        270        280        290        300 
LIVTGALVGS SGAILSYIMC KAMNRSFISV IAGGFGTDGS STGDDQEVGE HREITAEETA 

       310        320        330        340        350        360 
ELLKNSHSVI ITPGYGMAVA QAQYPVAEIT EKLRARGINV RFGIHPVAGR LPGHMNVLLA 

       370        380        390        400        410        420 
EAKVPYDIVL EMDEINDDFA DTDTVLVIGA NDTVNPAAQD DPKSPIAGMP VLEVWKAQNV 

       430        440        450        460 
IVFKRSMNTG YAGVQNPLFF KENTHMLFGD AKASVDAILK AL

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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. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed: 11206551] [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. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

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Cross-references

Sequence databases

AE005174 Genomic DNA. Translation: AAG56589.1.
BA000007 Genomic DNA. Translation: BAB35731.1.
PIRA85766.
D90917.
RefSeqNP_288037.1.
NP_310335.1.

3D structure databases

HSSPHSSP built from PDB template 1D4O based on UniProtKB P11024.
SMRP0AB69. Positions 296-462.
ModBaseSearch...

Genome annotation databases

GeneID913582.
961550.
GenomeReviewsGene locus Z2597 in contig AE005174_GR.
Gene locus ECs2308 in contig BA000007_GR.
KEGGece:Z2597.
ecs:ECs2308.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP0AB69.
OMAP0AB69. VEIYVGI.

Enzyme and pathway databases

BioCycECOL83334:ECS2308-MON.

Family and domain databases

InterProIPR012136. NADH_DH_b.
IPR004003. NADP_transhyd_b.
[Graphical view]
PfamPF02233. PNTB. 1 hit.
[Graphical view]
PIRSFPIRSF000204. PNTB. 1 hit.
ProtoNetSearch...

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Entry information

Entry namePNTB_ECO57
AccessionPrimary (citable) accession number: P0AB69
Secondary accession number(s): P07002, P76890
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 8, 2005
Last modified: June 16, 2009
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents