ID Q19KD3_ENTCL Unreviewed; 462 AA.
AC Q19KD3;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 102.
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:ABF71059.1};
GN ORFNames=J5T73_001393 {ECO:0000313|EMBL:HAZ4813211.1}, N5E88_14690
GN {ECO:0000313|EMBL:MDH1480721.1};
OS Enterobacter cloacae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX NCBI_TaxID=550 {ECO:0000313|EMBL:ABF71059.1};
RN [1] {ECO:0000313|EMBL:ABF71059.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SLD1a-1 {ECO:0000313|EMBL:ABF71059.1};
RA Dalia A.B., Yee N., Kobayashi D.Y.;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABF71059.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SLD1a-1 {ECO:0000313|EMBL:ABF71059.1};
RX PubMed=17261520; DOI=10.1128/AEM.02542-06;
RA Yee N., Ma J., Dalia A., Boonfueng T., Kobayashi D.Y.;
RT "Se(VI) reduction and the precipitation of Se(0) by the facultative
RT bacterium Enterobacter cloacae SLD1a-1 are regulated by FNR.";
RL Appl. Environ. Microbiol. 73:1914-1920(2007).
RN [3] {ECO:0000313|EMBL:HAZ4813211.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C041 {ECO:0000313|EMBL:HAZ4813211.1};
RX PubMed=30286803;
RA Souvorov A., Agarwala R., Lipman D.J.;
RT "SKESA: strategic k-mer extension for scrupulous assemblies.";
RL Genome Biol. 19:153-153(2018).
RN [4] {ECO:0000313|EMBL:HAZ4813211.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C041 {ECO:0000313|EMBL:HAZ4813211.1};
RG NCBI Pathogen Detection Project;
RL Submitted (MAR-2021) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:MDH1480721.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GD03711 {ECO:0000313|EMBL:MDH1480721.1};
RA Diorio-Toth L.;
RT "Intensive care unit water sources are persistently colonized with multi-
RT drug resistant bacteria and are the site of extensive horizontal gene
RT transfer of antibiotic resistance genes.";
RL Submitted (SEP-2022) to the EMBL/GenBank/DDBJ databases.
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; DQ523830; ABF71059.1; -; Genomic_DNA.
DR EMBL; DADOIZ010000002; HAZ4813211.1; -; Genomic_DNA.
DR EMBL; JAOCIY010000040; MDH1480721.1; -; Genomic_DNA.
DR RefSeq; WP_013096868.1; NZ_VWXR01000003.1.
DR GeneID; 83674757; -.
DR PATRIC; fig|550.124.peg.1197; -.
DR OMA; NDVVNPQ; -.
DR Proteomes; UP000868535; Unassembled WGS sequence.
DR Proteomes; UP001161707; Unassembled WGS sequence.
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 GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
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 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..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 36..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 7..460
FT /note="NADP transhydrogenase beta-like"
FT /evidence="ECO:0000259|Pfam:PF02233"
SQ SEQUENCE 462 AA; 48887 MW; A1B6BEA865922C3F CRC64;
MSGGLVTAAY IVAAILFIFS LAGLSKHETS QQGNNFGIAG MAIALIATIF GPDTGNVAWI
LVAMIIGGAI GIRLAKRVEM TEMPELVAIL HSFVGLAAVL VGFNSYLYHE PGMEPILVNI
HLTEVFLGIF IGAVTFTGSI VAFGKLRGKI SSKPLMLPNR HKLNLAALVV SFVLLVVFVR
TESVGLQVLA LLVMTIIALA FGWHLVASIG GADMPVVVSM LNSYSGWAAA AAGFMLSNDL
LIVTGALVGS SGAILSYIMC KAMNRSFISV IAGGFGSDGS STGSDEEVGE HREISAEDTA
EMLKNSHSVI ITPGYGMAVA QAQYPVAEIT EKLRARGIKV RFGIHPVAGR LPGHMNVLLA
EAKVPYDIVL EMDEINDDFA DTDTVLVIGA NDTVNPAAQD DPRSPIAGMP VLEVWKAQNV
IVFKRSMNTG YAGVQNPLFF KENTHMLFGD AKASVDAILK AL
//
