ID PNTAB_RICPR Reviewed; 132 AA. AC P51995; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 28-JAN-2026, entry version 107. 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=Pyridine nucleotide transhydrogenase subunit alpha 2; GN Name=pntAB; OrderedLocusNames=RP862; OS Rickettsia prowazekii (strain Madrid E). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; typhus group. OX NCBI_TaxID=272947; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Madrid E; RA Wood D.O., Marks G.L., Winkler H.H.; RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Madrid E; RX PubMed=9823893; DOI=10.1038/24094; RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., RA Kurland C.G.; RT "The genome sequence of Rickettsia prowazekii and the origin of RT mitochondria."; RL Nature 396:133-140(1998). RN [3] RP IDENTIFICATION, AND GENE NAME. RX PubMed=8662004; DOI=10.1007/bf02352282; RA Andersson S.G.E., Sharp P.M.; RT "Codon usage and base composition in Rickettsia prowazekii."; RL J. Mol. Evol. 42:525-536(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 Evidence={ECO:0000250|UniProtKB:Q2RSB2}; CC -!- SUBUNIT: Complex of an alpha and a beta chain; in Rickettsia, the alpha CC chain seems to be made of two subunits. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000250}. 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; U02878; -; NOT_ANNOTATED_CDS; Unassigned_DNA. DR EMBL; AJ235273; CAA15286.1; -; Genomic_DNA. DR PIR; F71648; F71648. DR RefSeq; WP_004596754.1; NC_000963.1. DR AlphaFoldDB; P51995; -. DR SMR; P51995; -. DR STRING; 272947.gene:17555931; -. DR EnsemblBacteria; CAA15286; CAA15286; CAA15286. DR GeneID; 57569985; -. DR KEGG; rpr:RP862; -. DR PATRIC; fig|272947.5.peg.901; -. DR eggNOG; COG3288; Bacteria. DR HOGENOM; CLU_137885_0_0_5; -. DR OrthoDB; 9810841at2; -. DR Proteomes; UP000002480; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0050661; F:NADP binding; IEA:TreeGrafter. DR GO; GO:0008750; F:proton-translocating NAD(P)+ transhydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0006740; P:NADPH regeneration; IEA:TreeGrafter. DR InterPro; IPR024605; NADP_transhyd_a_C. DR PANTHER; PTHR10160; NAD(P) TRANSHYDROGENASE; 1. DR PANTHER; PTHR10160:SF19; PROTON-TRANSLOCATING NAD(P)(+) TRANSHYDROGENASE; 1. 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..132 FT /note="NAD(P) transhydrogenase subunit alpha part 2" FT /id="PRO_0000199022" FT TRANSMEM 43..63 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 72..92 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 103..123 FT /note="Helical" FT /evidence="ECO:0000255" SQ SEQUENCE 132 AA; 14325 MW; 8A56163C9F394F0D CRC64; MNQLPIMAKQ AAEIASNAQE LSNKLKDLVI DASWQTNTNT IDPLVFAITI FVLASFVGYY VVWKVTPALH TPLMSITNAI SGIIVISSMI AITSSSAFEF SSLLGSFATL LASINIFGGF IVTTRMLEMF KK //