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   16-JUN-2009, entry version 44.
DE   RecName: Full=NAD(P) transhydrogenase subunit alpha part 2;
DE            EC=1.6.1.2;
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.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=782;
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   MEDLINE=99039499; PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O.,
RA   Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K.,
RA   Eriksson A.-S., Winkler H.H., 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   MEDLINE=96259307; 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
CC       to respiration and ATP hydrolysis and functions as a proton pump
CC       across the membrane (By similarity).
CC   -!- CATALYTIC ACTIVITY: NADPH + NAD(+) = NADP(+) + NADH.
CC   -!- SUBUNIT: Complex of an alpha and a beta chain; in Rickettsia, the
CC       alpha chain seems to be made of two subunits.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein (By similarity).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U02878; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR   EMBL; AJ235273; CAA15286.1; -; Genomic_DNA.
DR   PIR; F71648; F71648.
DR   RefSeq; NP_221210.1; -.
DR   GeneID; 883350; -.
DR   GenomeReviews; AJ235269_GR; RP862.
DR   KEGG; rpr:RP862; -.
DR   HOGENOM; P51995; -.
DR   OMA; P51995; MELVNHT.
DR   BioCyc; RPRO272947:RP862-MON; -.
DR   BRENDA; 1.6.1.2; 141977.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) acti...; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Complete proteome; Membrane; NAD;
KW   NADP; Oxidoreductase; Transmembrane.
FT   CHAIN         1    132       NAD(P) transhydrogenase subunit alpha
FT                                part 2.
FT                                /FTId=PRO_0000199022.
FT   TRANSMEM     43     63       Potential.
FT   TRANSMEM     72     92       Potential.
FT   TRANSMEM    103    123       Potential.
SQ   SEQUENCE   132 AA;  14325 MW;  8A56163C9F394F0D CRC64;
     MNQLPIMAKQ AAEIASNAQE LSNKLKDLVI DASWQTNTNT IDPLVFAITI FVLASFVGYY
     VVWKVTPALH TPLMSITNAI SGIIVISSMI AITSSSAFEF SSLLGSFATL LASINIFGGF
     IVTTRMLEMF KK
//