ID PNTB_ECOL6 Reviewed; 462 AA.
AC P0AB68; P07002; P76890;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 99.
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=c1994;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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. {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PNT beta subunit family. {ECO:0000305}.
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DR EMBL; AE014075; AAN80454.1; -; Genomic_DNA.
DR RefSeq; WP_000014036.1; NZ_CP051263.1.
DR AlphaFoldDB; P0AB68; -.
DR BMRB; P0AB68; -.
DR SMR; P0AB68; -.
DR STRING; 199310.c1994; -.
DR GeneID; 75204446; -.
DR KEGG; ecc:c1994; -.
DR eggNOG; COG1282; Bacteria.
DR HOGENOM; CLU_007866_4_0_6; -.
DR BioCyc; ECOL199310:C1994-MONOMER; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR012136; NADH_DH_b.
DR InterPro; IPR034300; PNTB-like.
DR PANTHER; PTHR44758; NAD(P) TRANSHYDROGENASE SUBUNIT BETA; 1.
DR PANTHER; PTHR44758:SF1; NAD(P) TRANSHYDROGENASE SUBUNIT BETA; 1.
DR Pfam; PF02233; PNTB; 1.
DR PIRSF; PIRSF000204; PNTB; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; NAD; NADP;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..462
FT /note="NAD(P) transhydrogenase subunit beta"
FT /id="PRO_0000199025"
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"
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
//
