PNTB_ECOLI
ID PNTB_ECOLI Reviewed; 462 AA.
AC P0AB67; P07002; P76890;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=NAD(P) transhydrogenase subunit beta;
DE EC=7.1.1.1;
DE AltName: Full=Nicotinamide nucleotide transhydrogenase subunit beta;
DE AltName: Full=Pyridine nucleotide transhydrogenase subunit beta;
GN Name=pntB; OrderedLocusNames=b1602, JW1594;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3525165; DOI=10.1111/j.1432-1033.1986.tb09802.x;
RA Clarke D.M., Loo T.W., Gillam S., Bragg P.D.;
RT "Nucleotide sequence of the pntA and pntB genes encoding the pyridine
RT nucleotide transhydrogenase of Escherichia coli.";
RL Eur. J. Biochem. 158:647-653(1986).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=1633824; DOI=10.1111/j.1432-1033.1992.tb17103.x;
RA Ahmad S., Glavas N.A., Bragg P.D.;
RT "A mutation at Gly314 of the beta subunit of the Escherichia coli pyridine
RT nucleotide transhydrogenase abolishes activity and affects the NADP(H)-
RT induced conformational change.";
RL Eur. J. Biochem. 207:733-739(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 266-277 AND 364-373.
RX PubMed=1932078; DOI=10.1016/0167-4838(91)90106-a;
RA Tong R.C., Glavas N.A., Bragg P.D.;
RT "Topological analysis of the pyridine nucleotide transhydrogenase of
RT Escherichia coli using proteolytic enzymes.";
RL Biochim. Biophys. Acta 1080:19-28(1991).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: The transhydrogenation between NADH and NADP is coupled to
CC respiration and ATP hydrolysis and functions as a proton pump across
CC the membrane.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + NAD(+) + NADPH = H(+)(out) + NADH + NADP(+);
CC Xref=Rhea:RHEA:47992, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57945, ChEBI:CHEBI:58349; EC=7.1.1.1;
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the PNT beta subunit family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X04195; CAB37090.1; -; Genomic_DNA.
DR EMBL; X66086; CAA46885.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74674.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15336.1; -; Genomic_DNA.
DR PIR; S24381; DEECXB.
DR RefSeq; NP_416119.1; NC_000913.3.
DR RefSeq; WP_000014036.1; NZ_STEB01000003.1.
DR PDB; 2BRU; NMR; -; C=286-462.
DR PDBsum; 2BRU; -.
DR AlphaFoldDB; P0AB67; -.
DR BMRB; P0AB67; -.
DR SMR; P0AB67; -.
DR BioGRID; 4259125; 34.
DR ComplexPortal; CPX-5623; NAD(P) transhydrogenase complex.
DR DIP; DIP-367N; -.
DR STRING; 511145.b1602; -.
DR TCDB; 3.D.2.1.1; the proton-translocating transhydrogenase (pth) family.
DR jPOST; P0AB67; -.
DR PaxDb; P0AB67; -.
DR PRIDE; P0AB67; -.
DR EnsemblBacteria; AAC74674; AAC74674; b1602.
DR EnsemblBacteria; BAA15336; BAA15336; BAA15336.
DR GeneID; 66674507; -.
DR GeneID; 946144; -.
DR KEGG; ecj:JW1594; -.
DR KEGG; eco:b1602; -.
DR PATRIC; fig|1411691.4.peg.660; -.
DR EchoBASE; EB0738; -.
DR eggNOG; COG1282; Bacteria.
DR HOGENOM; CLU_007866_4_0_6; -.
DR InParanoid; P0AB67; -.
DR OMA; KRGMSAG; -.
DR PhylomeDB; P0AB67; -.
DR BioCyc; EcoCyc:PNTB-MON; -.
DR BioCyc; MetaCyc:PNTB-MON; -.
DR EvolutionaryTrace; P0AB67; -.
DR PRO; PR:P0AB67; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0009327; C:NAD(P)+ transhydrogenase complex (AB-specific); IPI:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) activity; IDA:EcoCyc.
DR GO; GO:0008746; F:NAD(P)+ transhydrogenase activity; IDA:EcoCyc.
DR GO; GO:0050661; F:NADP binding; IDA:EcoCyc.
DR GO; GO:0006740; P:NADPH regeneration; IDA:ComplexPortal.
DR GO; GO:0120029; P:proton export across plasma membrane; IDA:ComplexPortal.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR012136; NADH_DH_b.
DR InterPro; IPR034300; PNTB-like.
DR Pfam; PF02233; PNTB; 1.
DR PIRSF; PIRSF000204; PNTB; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Membrane; NAD; NADP; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..462
FT /note="NAD(P) transhydrogenase subunit beta"
FT /id="PRO_0000199023"
FT TOPO_DOM 1..3
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..82
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..164
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..215
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..308
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..462
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT HELIX 297..305
FT /evidence="ECO:0007829|PDB:2BRU"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:2BRU"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:2BRU"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:2BRU"
FT HELIX 323..336
FT /evidence="ECO:0007829|PDB:2BRU"
FT STRAND 339..344
FT /evidence="ECO:0007829|PDB:2BRU"
FT STRAND 346..353
FT /evidence="ECO:0007829|PDB:2BRU"
FT HELIX 355..362
FT /evidence="ECO:0007829|PDB:2BRU"
FT TURN 366..368
FT /evidence="ECO:0007829|PDB:2BRU"
FT STRAND 369..372
FT /evidence="ECO:0007829|PDB:2BRU"
FT HELIX 376..381
FT /evidence="ECO:0007829|PDB:2BRU"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:2BRU"
FT HELIX 391..394
FT /evidence="ECO:0007829|PDB:2BRU"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:2BRU"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:2BRU"
FT STRAND 417..423
FT /evidence="ECO:0007829|PDB:2BRU"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:2BRU"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:2BRU"
FT STRAND 440..447
FT /evidence="ECO:0007829|PDB:2BRU"
FT HELIX 451..461
FT /evidence="ECO:0007829|PDB:2BRU"
SQ SEQUENCE 462 AA; 48723 MW; D11747291D271A2F CRC64;
MSGGLVTAAY IVAAILFIFS LAGLSKHETS RQGNNFGIAG MAIALIATIF GPDTGNVGWI
LLAMVIGGAI GIRLAKKVEM TEMPELVAIL HSFVGLAAVL VGFNSYLHHD AGMAPILVNI
HLTEVFLGIF IGAVTFTGSV VAFGKLCGKI SSKPLMLPNR HKMNLAALVV SFLLLIVFVR
TDSVGLQVLA LLIMTAIALV FGWHLVASIG GADMPVVVSM LNSYSGWAAA AAGFMLSNDL
LIVTGALVGS SGAILSYIMC KAMNRSFISV IAGGFGTDGS STGDDQEVGE HREITAEETA
ELLKNSHSVI ITPGYGMAVA QAQYPVAEIT EKLRARGINV RFGIHPVAGR LPGHMNVLLA
EAKVPYDIVL EMDEINDDFA DTDTVLVIGA NDTVNPAAQD DPKSPIAGMP VLEVWKAQNV
IVFKRSMNTG YAGVQNPLFF KENTHMLFGD AKASVDAILK AL
