NUOL_PSEAE
ID NUOL_PSEAE Reviewed; 615 AA.
AC Q9I0J1;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=NADH-quinone oxidoreductase subunit L;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I subunit L;
DE AltName: Full=NDH-1 subunit L;
GN Name=nuoL; OrderedLocusNames=PA2647;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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 believed to be
CC ubiquinone. Couples the redox reaction to proton translocation (for
CC every two electrons transferred, four hydrogen ions are translocated
CC across the cytoplasmic membrane), and thus conserves the redox energy
CC in a proton gradient (By similarity). {ECO:0000250}.
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 -!- SUBUNIT: Composed of 13 different subunits. Subunits NuoA, H, J, K, L,
CC M, N constitute the membrane sector of the complex (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the complex I subunit 5 family. {ECO:0000305}.
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DR EMBL; AE004091; AAG06035.1; -; Genomic_DNA.
DR PIR; D83315; D83315.
DR RefSeq; NP_251337.1; NC_002516.2.
DR RefSeq; WP_003097681.1; NZ_QZGE01000008.1.
DR AlphaFoldDB; Q9I0J1; -.
DR SMR; Q9I0J1; -.
DR STRING; 287.DR97_5315; -.
DR PaxDb; Q9I0J1; -.
DR PRIDE; Q9I0J1; -.
DR EnsemblBacteria; AAG06035; AAG06035; PA2647.
DR GeneID; 882356; -.
DR KEGG; pae:PA2647; -.
DR PATRIC; fig|208964.12.peg.2770; -.
DR PseudoCAP; PA2647; -.
DR HOGENOM; CLU_007100_6_2_6; -.
DR InParanoid; Q9I0J1; -.
DR OMA; GVGIMSF; -.
DR PhylomeDB; Q9I0J1; -.
DR BioCyc; PAER208964:G1FZ6-2687-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0045272; C:plasma membrane respiratory chain complex I; IBA:GO_Central.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0003954; F:NADH dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR InterPro; IPR018393; NADHpl_OxRdtase_5_subgr.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR003945; NU5C-like.
DR InterPro; IPR001516; Proton_antipo_N.
DR PANTHER; PTHR42829; PTHR42829; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR Pfam; PF00662; Proton_antipo_N; 1.
DR TIGRFAMs; TIGR01974; NDH_I_L; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Ubiquinone.
FT CHAIN 1..615
FT /note="NADH-quinone oxidoreductase subunit L"
FT /id="PRO_0000287831"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 496..516
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 594..614
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 615 AA; 66228 MW; 10572A5724555E22 CRC64;
MNLLPLTFLF PLVGFLLLSF SRGRWSENLS ALVGVGSVGL SALSAAWAIF SFHSSPPEGG
AYSLVLWQWM AAGDFSTNFT LYLDGLSVTM LGVVTGVGFL IHLFASWYMR GETGYSRFFA
YTNLFIASML FLVLGDNLLF LYFGWEGVGL CSYLLIGFYY SNRNNGNAAL KAFIVTRVGD
VFMAFGLFIL FQQFGTLNIQ ELLVLAPQKF PEGNLWLTLA TLALLGGAVG KSAQLPLQTW
LADAMAGPTP VSALIHAATM VTAGVYLIAR CHGLFTLAPD ILELVGIVGA VTLVLAGFAA
LVQTDIKRIL AYSTMSQIGY MFLALGVGAW DAAIFHLMTH AFFKALLFLA SGAVIVACHH
EQNIFKMGGL WKKLPLAYAS FVVGGAALAA LPFLTAGFYS KDEILWEAFA SGHRELLIAG
LVGAFLTSIY TFRLIFVAFH GEPKTEAHAG HGISHWLPLS VLIVLSTFVG ALITPPLAGV
LPESVGHAGG EAKHSLELAS GAIAIAGILL AALLFLGQRR FVSALAKSAP GRFFGTWWYH
AWGFDWLYDK LFVKPYLLLC QLLGRDPIDR TLGVVPFSVR GGHNLLSLTE NGRLRWYAAS
LVGGAAILLG ALLLA
