ID   PNTAB_RHORT             Reviewed;         139 AA.
AC   Q2RSB3; Q59762; Q59764;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=NAD(P) transhydrogenase subunit alpha part 2;
DE            EC=7.1.1.1 {ECO:0000250|UniProtKB:Q2RSB2};
DE   AltName: Full=Nicotinamide nucleotide transhydrogenase subunit alpha 2;
DE   AltName: Full=Proton-translocating transhydrogenase component 2;
DE   AltName: Full=Pyridine nucleotide transhydrogenase subunit alpha 2;
DE   AltName: Full=dII;
GN   Name=pntAB; Synonyms=nntA2; OrderedLocusNames=Rru_A2182;
OS   Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS   NCIMB 8255 / S1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8075801; DOI=10.1099/13500872-140-7-1595;
RA   Williams R., Cotton N.P., Thomas C.M., Jackson J.B.;
RT   "Cloning and sequencing of the genes for the proton-translocating
RT   nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum and the
RT   implications for the domain structure of the enzyme.";
RL   Microbiology 140:1595-1604(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX   PubMed=21886856; DOI=10.4056/sigs.1804360;
RA   Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA   Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA   Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA   Roberts G.P., Reslewic S., Schwartz D.C.;
RT   "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL   Stand. Genomic Sci. 4:293-302(2011).
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         Evidence={ECO:0000250|UniProtKB:Q2RSB2};
CC   -!- SUBUNIT: Complex of an alpha and a beta chain; in Rhodospirillum, the
CC       alpha chain seems to be made of two subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
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DR   EMBL; U05294; AAA62494.1; -; Genomic_DNA.
DR   EMBL; CP000230; ABC22982.1; -; Genomic_DNA.
DR   RefSeq; WP_011390031.1; NC_007643.1.
DR   RefSeq; YP_427269.1; NC_007643.1.
DR   AlphaFoldDB; Q2RSB3; -.
DR   SMR; Q2RSB3; -.
DR   STRING; 269796.Rru_A2182; -.
DR   EnsemblBacteria; ABC22982; ABC22982; Rru_A2182.
DR   KEGG; rru:Rru_A2182; -.
DR   PATRIC; fig|269796.9.peg.2276; -.
DR   eggNOG; COG3288; Bacteria.
DR   HOGENOM; CLU_137885_0_0_5; -.
DR   OMA; TKNEAQK; -.
DR   OrthoDB; 1933548at2; -.
DR   PhylomeDB; Q2RSB3; -.
DR   Proteomes; UP000001929; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR024605; NADP_transhyd_a_C.
DR   Pfam; PF12769; PNTB_4TM; 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..139
FT                   /note="NAD(P) transhydrogenase subunit alpha part 2"
FT                   /id="PRO_0000231664"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   139 AA;  14889 MW;  04742D87817A8879 CRC64;
     MEDKNILVEG FNQLSQQALE LSQHAQALAL QASHAVLPAA AATEGASEFW WLMTVFVLAC
     FIGFYVVWSV TPALHSPLMG VTNAISSVIV VGALIATGPE AFSASKVLGF FAILLASVNI
     FGGFIVTQRM LAMFKKKQK