P0AB67 (PNTB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	b1602, JW1594

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	462 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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.
Catalytic activity	NADPH + NAD+ = NADP+ + NADH.
Subunit structure	Heterodimer of an alpha and a beta chain.
Subcellular location	Cell inner membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the PNT beta subunit family.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	NAD NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	NADPH regeneration Inferred from mutant phenotype PubMed 14660605. Source: EcoCyc
Cellular_component	integral to plasma membrane Inferred from direct assay PubMed 3884596. Source: EcoCyc
Molecular_function	NAD(P)+ transhydrogenase (AB-specific) activity Inferred from direct assay PubMed 19400036. Source: EcoCyc NADP binding Inferred from direct assay PubMed 11027139. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 462

462

NAD(P) transhydrogenase subunit beta

PRO_0000199023

Regions

Topological domain

1 – 3

3

Periplasmic Potential

Transmembrane

4 – 24

21

Helical; Potential

Topological domain

25 – 45

21

Cytoplasmic Potential

Transmembrane

46 – 66

21

Helical; Potential

Topological domain

67 – 82

16

Periplasmic Potential

Transmembrane

83 – 103

21

Helical; Potential

Topological domain

104 – 115

12

Cytoplasmic Potential

Transmembrane

116 – 136

21

Helical; Potential

Topological domain

137 – 164

28

Periplasmic Potential

Transmembrane

165 – 185

21

Helical; Potential

Topological domain

186 – 188

3

Cytoplasmic Potential

Transmembrane

189 – 209

21

Helical; Potential

Topological domain

210 – 215

6

Periplasmic Potential

Transmembrane

216 – 236

21

Helical; Potential

Topological domain

237 – 239

3

Cytoplasmic Potential

Transmembrane

240 – 260

21

Helical; Potential

Topological domain

261 – 308

48

Periplasmic Potential

Transmembrane

309 – 329

21

Helical; Potential

Topological domain

330 – 462

133

Cytoplasmic Potential

Secondary structure

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462

Helix Strand Turn

Details...

Helix

297 – 305

9

Beta strand

307 – 312

6

Helix

316 – 319

4

Turn

320 – 322

3

Helix

323 – 336

14

Beta strand

339 – 344

6

Beta strand

346 – 353

8

Helix

355 – 362

8

Turn

366 – 368

3

Beta strand

369 – 372

4

Helix

376 – 381

6

Beta strand

383 – 387

5

Helix

391 – 394

4

Helix

396 – 398

3

Beta strand

404 – 406

3

Beta strand

417 – 423

7

Beta strand

425 – 427

3

Turn

437 – 439

3

Beta strand

440 – 447

8

Helix

451 – 461

11

Sequences

	Sequence		Length	Mass (Da)
	P0AB67 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: D11747291D271A2F	FASTA	462	48,723
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the pntA and pntB genes encoding the pyridine nucleotide transhydrogenase of Escherichia coli." Clarke D.M., Loo T.W., Gillam S., Bragg P.D. Eur. J. Biochem. 158:647-653(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"A mutation at Gly314 of the beta subunit of the Escherichia coli pyridine nucleotide transhydrogenase abolishes activity and affects the NADP(H)-induced conformational change." Ahmad S., Glavas N.A., Bragg P.D. Eur. J. Biochem. 207:733-739(1992) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[3]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"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.
[5]	"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.
[6]	"Topological analysis of the pyridine nucleotide transhydrogenase of Escherichia coli using proteolytic enzymes." Tong R.C., Glavas N.A., Bragg P.D. Biochim. Biophys. Acta 1080:19-28(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 266-277 AND 364-373.
[7]	"Global topology analysis of the Escherichia coli inner membrane proteome." Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G. Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS]. Strain: K12 / MG1655 / ATCC 47076.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X04195 Genomic DNA. Translation: CAB37090.1.
X66086 Genomic DNA. Translation: CAA46885.1.
U00096 Genomic DNA. Translation: AAC74674.1.
AP009048 Genomic DNA. Translation: BAA15336.1.

PIR

DEECXB. S24381.

RefSeq

NP_416119.1. NC_000913.2.
YP_489865.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BRU	NMR	-	C	286-462	[»]

ProteinModelPortal

P0AB67.

SMR

P0AB67. Positions 296-462.

ModBase

Search...

Protein-protein interaction databases

STRING

511145.b1602.

Protein family/group databases

TCDB

3.D.2.1.1. proton-translocating transhydrogenase (PTH) family.

Proteomic databases

PaxDb

P0AB67.

PRIDE

P0AB67.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74674; AAC74674; b1602.
BAA15336; BAA15336; BAA15336.

GeneID

12930131.
946144.

KEGG

ecj:Y75_p1578.
eco:b1602.

PATRIC

32118506. VBIEscCol129921_1673.

Organism-specific databases

EchoBASE

EB0738.

EcoGene

EG10745. pntB.

Phylogenomic databases

eggNOG

COG1282.

HOGENOM

HOG000243958.

KO

K00325.

OMA

GNVGWII.

ProtClustDB

PRK09444.

Enzyme and pathway databases

BioCyc

EcoCyc:PNTB-MONOMER.
ECOL316407:JW1594-MONOMER.
MetaCyc:PNTB-MONOMER.

Gene expression databases

Genevestigator

P0AB67.

Family and domain databases

InterPro

IPR012136. NADH_DH_b.
[Graphical view]

Pfam

PF02233. PNTB. 1 hit.
[Graphical view]

PIRSF

PIRSF000204. PNTB. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P0AB67.

Entry information

Entry name

PNTB_ECOLI

Accession

Primary (citable) accession number: P0AB67
Secondary accession number(s): P07002, P76890

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	November 8, 2005
Last modified:	May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program