ID K9RTR5_SYNP3 Unreviewed; 618 AA.
AC K9RTR5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=NAD(P)H dehydrogenase, subunit NdhF3 family {ECO:0000313|EMBL:AFY60911.1};
GN OrderedLocusNames=Syn6312_1762 {ECO:0000313|EMBL:AFY60911.1};
OS Synechococcus sp. (strain ATCC 27167 / PCC 6312).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=195253 {ECO:0000313|EMBL:AFY60911.1, ECO:0000313|Proteomes:UP000010379};
RN [1] {ECO:0000313|Proteomes:UP000010379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27167 / PCC 6312 {ECO:0000313|Proteomes:UP000010379};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC -!- FUNCTION: NDH-1 shuttles electrons from NAD(P)H, via FMN and iron-
CC sulfur (Fe-S) centers, to quinones in the respiratory chain. The
CC immediate electron acceptor for the enzyme in this species is believed
CC to be plastoquinone. Couples the redox reaction to proton translocation
CC (for every two electrons transferred, four hydrogen ions are
CC translocated across the cytoplasmic membrane), and thus conserves the
CC redox energy in a proton gradient. {ECO:0000256|ARBA:ARBA00025624}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU000320}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU000320}.
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DR EMBL; CP003558; AFY60911.1; -; Genomic_DNA.
DR RefSeq; WP_015124454.1; NC_019680.1.
DR AlphaFoldDB; K9RTR5; -.
DR STRING; 195253.Syn6312_1762; -.
DR KEGG; syne:Syn6312_1762; -.
DR PATRIC; fig|195253.3.peg.1796; -.
DR eggNOG; COG1009; Bacteria.
DR HOGENOM; CLU_007100_6_3_3; -.
DR OrthoDB; 9807568at2; -.
DR Proteomes; UP000010379; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR Gene3D; 1.20.5.2700; -; 1.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR003945; NU5C-like.
DR InterPro; IPR010217; NU5C2.
DR InterPro; IPR001516; Proton_antipo_N.
DR NCBIfam; TIGR01960; ndhF3_CO2; 1.
DR PANTHER; PTHR42829; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1.
DR PANTHER; PTHR42829:SF2; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR Pfam; PF00662; Proton_antipo_N; 1.
DR PRINTS; PR01434; NADHDHGNASE5.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Quinone {ECO:0000256|ARBA:ARBA00022719};
KW Reference proteome {ECO:0000313|Proteomes:UP000010379};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000320};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 39..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 219..244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 256..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 414..431
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 452..476
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 488..510
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 590..607
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..123
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 139..419
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 618 AA; 66213 MW; 47168C798E2B7BB7 CRC64;
MADILVATSW LVPCYGLLGA LATLPWATGW IKRTGPRPAA YLNFSLTFIA FVHGLLVFRI
LEATGPTELI WHWLSAPGLD IAFPLSITPL SVGAMELVTG LSLLAQLFAL GYMEKDWGLG
RFFALMGFFE AALSGLALSN SLLLSYMLLE LLTLSTYLLV GFWYAQPLVV TAARDAFLTK
RVGDILLLMG VVALATQAGS LDFPVLYDWA ENANLSPGLG FLLGLALIAG PTGKCAQFPL
HLWLDEAMEG PNPASIMRNS VVVGAGAYVL IKLQPILVHC YGSDVILITL GAVTAIGASL
VAMAQIDVKR ALSHSTSAYL GLVFVAVGCQ WINVAYLVLL THGIAKALLF MTMGCVINTT
NCQDLTELGG LGKRMPATVT GFVVGSAALV GVLPLGGFWA GYRVITRVGF ENPGLVAVML
IVNALTALNL MRMMRLVFLG QAQPKTRRAP EVPWPMAVPL VSLTILCVLV PVILARFQLL
PLAADLDWTA VVLLTGSGII GMAAGGLVNL NRTWSRPLQG QLRFLQDLFA YDFYVDRLYR
VTVVAGVQIL SQLSTWLDRY VVDNVVNLTG RAALAGGEFL KYGTGGQSQA YLILIFSALL
VAGLFLVKPL GMTFGWGG
//
