ID   PNTB_HAEIN              Reviewed;         474 AA.
AC   P43010;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   04-NOV-2026, entry version 135.
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=HI_1363;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pasteurellales; Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 244-474.
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=8635745; DOI=10.1016/0378-1119(95)00777-6;
RA   Chandler M.S., Smith R.A.;
RT   "Characterization of the Haemophilus influenzae topA locus: DNA
RT   topoisomerase I is required for genetic competence.";
RL   Gene 169:25-31(1996).
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=NAD(+) + NADPH + H(+)(in) = NADH + NADP(+) + H(+)(out);
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; L42023; AAC23010.1; -; Genomic_DNA.
DR   EMBL; U20964; AAC43725.1; -; Genomic_DNA.
DR   PIR; F64119; F64119.
DR   AlphaFoldDB; P43010; -.
DR   SMR; P43010; -.
DR   STRING; 71421.HI_1363; -.
DR   DNASU; 950280; -.
DR   EnsemblBacteria; AAC23010; AAC23010; HI_1363.
DR   KEGG; hin:HI_1363; -.
DR   PATRIC; fig|71421.8.peg.1417; -.
DR   eggNOG; COG1282; Bacteria.
DR   HOGENOM; CLU_007866_4_0_6; -.
DR   OMA; AADNHLM; -.
DR   OrthoDB; 9763786at2; -.
DR   PhylomeDB; P43010; -.
DR   BioCyc; HINF71421:G1GJ1-1388-MONOMER; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0008750; F:proton-translocating NAD(P)+ transhydrogenase activity; IBA:GO_Central.
DR   GO; GO:0006740; P:NADPH regeneration; IBA:GO_Central.
DR   GO; GO:0120029; P:proton export across plasma membrane; IBA:GO_Central.
DR   FunFam; 3.40.50.1220:FF:000002; NAD(P) transhydrogenase subunit beta; 1.
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   NCBIfam; NF006974; pntB; 1.
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..474
FT                   /note="NAD(P) transhydrogenase subunit beta"
FT                   /id="PRO_0000199026"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        229..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        253..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        321..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        343
FT                   /note="A -> P (in Ref. 2; AAC43725)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   474 AA;  50163 MW;  5F914630211FF844 CRC64;
     MSEGLVQAAY ILAALLFIMS LAGLSKHETA KAGCWFGIVG MTIALIATIF GPHSEGTFWI
     IIAMIIGGAI GVQRALKVEM TEMPELVAIL HSFVGLAAVL VGFNSYGLHH EALMPEGLDA
     AAQAAFVAEQ AVLTNIHNVE VFLGIFIGAV TFTGSVVAFG KLSGKINSKA LMLPHRHKLN
     LAALVVSALL MVAFLNNPES IFPVLLMTAI ALAFGWHLVA SIGGADMPVV VSMLNSYSGW
     AAAAAGFILN NDLLIVTGAL VGSSGAILSY IMCKAMNRSF VSVIAGGFGN DVQVSSSEEQ
     GEHRETTAEE VAELLKNASS VIITPGYGMA VAQAQYPVAD ITAKLRERGV NVRFGIHPVA
     GRLPGHMNVL LAEAKVPYDV VLEMDEINDD FADTDVVLVI GANDTVNPAA MEDPNSPIAG
     MPVLEVWKAQ NVIVFKRSMA VGYAGVQNPL FFKENTQMLF GDAKDRVEDI LKAL
//