NQO14_THET8
ID NQO14_THET8 Reviewed; 427 AA.
AC Q56229; Q5SM46;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=NADH-quinone oxidoreductase subunit 14;
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_00445};
DE AltName: Full=NADH dehydrogenase I chain 14;
DE AltName: Full=NDH-1 subunit 14;
GN Name=nqo14; OrderedLocusNames=TTHA0097;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=9020134; DOI=10.1074/jbc.272.7.4201;
RA Yano T., Chu S.S., Sled' V.D., Ohnishi T., Yagi T.;
RT "The proton-translocating NADH-quinone oxidoreductase (NDH-1) of
RT thermophilic bacterium Thermus thermophilus HB-8. Complete DNA sequence of
RT the gene cluster and thermostable properties of the expressed NQO2
RT subunit.";
RL J. Biol. Chem. 272:4201-4211(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC electron acceptor for the enzyme in this species is menaquinone.
CC Couples the redox reaction to proton translocation (for every two
CC electrons transferred, four hydrogen ions are translocated across the
CC cytoplasmic membrane), and thus conserves the redox energy in a proton
CC gradient required for the synthesis of ATP.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00445};
CC -!- SUBUNIT: NDH-1 is composed of 15 different subunits, Nqo1 to Nqo15. The
CC complex has a L-shaped structure, with the hydrophobic arm (subunits
CC Nqo7, Nqo8 and Nqo10 to Nqo14) embedded in the membrane and the
CC hydrophilic peripheral arm (subunits Nqo1 to Nqo6, Nqo9 and Nqo15)
CC protruding into the bacterial cytoplasm. The hydrophilic domain
CC contains all the redox centers.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the complex I subunit 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_00445}.
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DR EMBL; U52917; AAA97951.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD69920.1; -; Genomic_DNA.
DR PIR; T11911; T11911.
DR RefSeq; WP_011227707.1; NC_006461.1.
DR RefSeq; YP_143363.1; NC_006461.1.
DR PDB; 4HE8; X-ray; 3.30 A; I/N=1-427.
DR PDB; 4HEA; X-ray; 3.30 A; N/V=1-427.
DR PDB; 6I0D; X-ray; 3.60 A; N/V=1-427.
DR PDB; 6I1P; X-ray; 3.21 A; N/V=1-427.
DR PDB; 6Q8O; X-ray; 3.60 A; N/V=1-427.
DR PDB; 6Q8W; X-ray; 3.40 A; N/V=1-427.
DR PDB; 6Q8X; X-ray; 3.51 A; N/V=1-427.
DR PDB; 6Y11; X-ray; 3.11 A; N/V=1-427.
DR PDB; 6ZIY; EM; 4.25 A; N=1-427.
DR PDB; 6ZJL; EM; 4.30 A; N=1-427.
DR PDB; 6ZJN; EM; 6.10 A; N=1-427.
DR PDB; 6ZJY; EM; 5.50 A; N=1-427.
DR PDBsum; 4HE8; -.
DR PDBsum; 4HEA; -.
DR PDBsum; 6I0D; -.
DR PDBsum; 6I1P; -.
DR PDBsum; 6Q8O; -.
DR PDBsum; 6Q8W; -.
DR PDBsum; 6Q8X; -.
DR PDBsum; 6Y11; -.
DR PDBsum; 6ZIY; -.
DR PDBsum; 6ZJL; -.
DR PDBsum; 6ZJN; -.
DR PDBsum; 6ZJY; -.
DR AlphaFoldDB; Q56229; -.
DR SMR; Q56229; -.
DR DIP; DIP-59272N; -.
DR IntAct; Q56229; 1.
DR STRING; 300852.55771479; -.
DR TCDB; 3.D.1.3.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblBacteria; BAD69920; BAD69920; BAD69920.
DR GeneID; 3169623; -.
DR KEGG; ttj:TTHA0097; -.
DR PATRIC; fig|300852.9.peg.95; -.
DR eggNOG; COG1007; Bacteria.
DR HOGENOM; CLU_007100_1_5_0; -.
DR OMA; HFWVPEV; -.
DR PhylomeDB; Q56229; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR HAMAP; MF_00445; NDH1_NuoN_1; 1.
DR InterPro; IPR010096; NADH-Q_OxRdtase_suN/2.
DR InterPro; IPR001750; ND/Mrp_mem.
DR Pfam; PF00361; Proton_antipo_M; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..427
FT /note="NADH-quinone oxidoreductase subunit 14"
FT /id="PRO_0000117687"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT CONFLICT 81
FT /note="R -> G (in Ref. 1; AAA97951)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="A -> D (in Ref. 1; AAA97951)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="L -> V (in Ref. 1; AAA97951)"
FT /evidence="ECO:0000305"
FT CONFLICT 407..427
FT /note="VLLLALGLLPGLVLPALAAGG -> SSSSPWGSSPASSSPPWPRGVKITP
FT (in Ref. 1; AAA97951)"
FT /evidence="ECO:0000305"
FT HELIX 2..16
FT /evidence="ECO:0007829|PDB:6Y11"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 22..42
FT /evidence="ECO:0007829|PDB:6Y11"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 48..56
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 57..76
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 83..99
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 104..121
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 127..157
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 170..186
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 195..202
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 205..224
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 230..249
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 254..269
FT /evidence="ECO:0007829|PDB:6Y11"
FT TURN 270..276
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 279..302
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 315..318
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 320..334
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 340..354
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 359..379
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 380..383
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 396..414
FT /evidence="ECO:0007829|PDB:6Y11"
FT TURN 416..419
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:6Y11"
SQ SEQUENCE 427 AA; 44436 MW; 9AD943608E5C2759 CRC64;
MTLAILAVFS VALTLLGFVL PPQGVKRATL LGLALALASL LLTWGKPFAF GPYAVDGVSQ
VFTLLALLGA LWTVGLVRSG RFEFYLLVLY AALGMHLLAS TRHLLLMLVA LEALSLPLYA
LATWRRGQGL EAALKYFLLG ALAAAFFLYG AALFYGATGS LVLGAPGEGP LYALALGLLL
VGLGFKAALA PFHFWTPDVY QGSPTPVVLF MATSVKAAAF AALLRVAAPP EALALLVALS
VVVGNLAALA QKEAKRLLAY SSIAHAGYMA LALYTGNAQA LGFYLLTYVL ATGLAFAVLS
QISPDRVPLE ALRGLYRKDP LLGLAFLVAM LSLLGLPPLA GFWGKYLAFA EAARAGAWGV
LVLALVTSAV SAYYYLGLGL AVFARPEETP FRPGPPWARA AVVAAGVLLL ALGLLPGLVL
PALAAGG
