PNTAB_RICPR
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 25-MAY-2022, entry version 97.
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; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC 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=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 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}.
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DR EMBL; U02878; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; AJ235273; CAA15286.1; -; Genomic_DNA.
DR PIR; F71648; F71648.
DR RefSeq; NP_221210.1; NC_000963.1.
DR RefSeq; WP_004596754.1; NC_000963.1.
DR AlphaFoldDB; P51995; -.
DR SMR; P51995; -.
DR STRING; 272947.RP862; -.
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 OMA; FVVTDRM; -.
DR Proteomes; UP000002480; 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..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
