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Database: UniProt
Entry: D4ZJ20_SHEVD
LinkDB: D4ZJ20_SHEVD
Original site: D4ZJ20_SHEVD 
ID   D4ZJ20_SHEVD            Unreviewed;       466 AA.
AC   D4ZJ20;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=NAD(P) transhydrogenase subunit beta {ECO:0000256|ARBA:ARBA00014581, ECO:0000256|PIRNR:PIRNR000204};
DE            EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943, ECO:0000256|PIRNR:PIRNR000204};
DE   AltName: Full=Nicotinamide nucleotide transhydrogenase subunit beta {ECO:0000256|PIRNR:PIRNR000204};
GN   Name=pntB {ECO:0000313|EMBL:BAJ01669.1};
GN   OrderedLocusNames=SVI_1698 {ECO:0000313|EMBL:BAJ01669.1};
OS   Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 / DSS12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=637905 {ECO:0000313|EMBL:BAJ01669.1, ECO:0000313|Proteomes:UP000002350};
RN   [1] {ECO:0000313|Proteomes:UP000002350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10179 / CIP 106290 / LMG 19151 / DSS12
RC   {ECO:0000313|Proteomes:UP000002350};
RX   PubMed=20458400; DOI=10.1039/c000396d;
RA   Aono E., Baba T., Ara T., Nishi T., Nakamichi T., Inamoto E., Toyonaga H.,
RA   Hasegawa M., Takai Y., Okumura Y., Baba M., Tomita M., Kato C., Oshima T.,
RA   Nakasone K., Mori H.;
RT   "Complete genome sequence and comparative analysis of Shewanella violacea,
RT   a psychrophilic and piezophilic bacterium from deep sea floor sediments.";
RL   Mol. Biosyst. 6:1216-1226(2010).
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:0000256|ARBA:ARBA00003943,
CC       ECO:0000256|PIRNR:PIRNR000204}.
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:0000256|ARBA:ARBA00000006,
CC         ECO:0000256|PIRNR:PIRNR000204};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the PNT beta subunit family.
CC       {ECO:0000256|ARBA:ARBA00007919, ECO:0000256|PIRNR:PIRNR000204}.
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DR   EMBL; AP011177; BAJ01669.1; -; Genomic_DNA.
DR   RefSeq; WP_013050976.1; NC_014012.1.
DR   AlphaFoldDB; D4ZJ20; -.
DR   STRING; 637905.SVI_1698; -.
DR   KEGG; svo:SVI_1698; -.
DR   eggNOG; COG1282; Bacteria.
DR   HOGENOM; CLU_007866_4_0_6; -.
DR   OrthoDB; 9763786at2; -.
DR   Proteomes; UP000002350; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
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   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 {ECO:0000256|ARBA:ARBA00022519,
KW   ECO:0000256|PIRNR:PIRNR000204};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|PIRNR:PIRNR000204};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000204};
KW   NAD {ECO:0000256|PIRNR:PIRNR000204};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000204};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002350};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|PIRNR:PIRNR000204};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        35..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        58..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        89..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        133..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        164..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        192..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        220..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        244..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          8..464
FT                   /note="NADP transhydrogenase beta-like"
FT                   /evidence="ECO:0000259|Pfam:PF02233"
SQ   SEQUENCE   466 AA;  48651 MW;  49ECFF9342B3D1A4 CRC64;
     MSIGLLSAAY LIAAVLFIFS LAGLSKQETA QRGNLLGIIG MVIAVVATLA STQVGGNSWI
     ITVAMAIGAG IGIRLALKVE MTEMPELVAI LHSFVGLAAV LVGFSSALDH SILMDAVTGN
     IDPVAKTIHD VEVFLGIFIG GVTFTGSIVA FAKLRGLVKS TPKSLPGAHW LNLAMLVASV
     VLGIYYMQTD AISALVLMTA ISFVFGYNLV SAIGGADMPV VVSMLNSYSG WAAAAAGFML
     GNDLLIITGA LVGSSGAILS YIMCKAMNRS FISVILGGFG TSGGTVVIGD GELGEHRETQ
     AADVAELLKN ARTVIIAPGY GMAVAQAQYP VAEITKKLRD RGVKVRFAIH PVAGRLPGHM
     NVLLAEAKLP YDIVMEMDEI NDDFANTDVV LVIGANDTVN PAAKEPGSPI AGMPVLEVWN
     ADNVVVFKRS MATGYAGVQN PLFFKENTEM LFGDAKDSVS KILASI
//
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