NUOL_NEIMB
ID NUOL_NEIMB Reviewed; 674 AA.
AC Q9K1B0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 107.
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=NMB0257;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the complex I subunit 5 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE002098; AAF40711.1; -; Genomic_DNA.
DR PIR; D81220; D81220.
DR RefSeq; NP_273313.1; NC_003112.2.
DR RefSeq; WP_002221913.1; NC_003112.2.
DR AlphaFoldDB; Q9K1B0; -.
DR SMR; Q9K1B0; -.
DR STRING; 122586.NMB0257; -.
DR PaxDb; Q9K1B0; -.
DR EnsemblBacteria; AAF40711; AAF40711; NMB0257.
DR KEGG; nme:NMB0257; -.
DR PATRIC; fig|122586.8.peg.320; -.
DR HOGENOM; CLU_007100_6_0_4; -.
DR OMA; LIGFWQH; -.
DR Proteomes; UP000000425; 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: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 membrane; Membrane; NAD; Quinone; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Ubiquinone.
FT CHAIN 1..674
FT /note="NADH-quinone oxidoreductase subunit L"
FT /id="PRO_0000118220"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 549..569
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 653..673
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 674 AA; 74229 MW; C915DA24F0FDE5A3 CRC64;
MNDMTLYLII ALVPLAGSLI AGLFGNKIGR AGAHTVTILG VAVSAVLSAY VLWGFIDGSR
AKFDENVYTW LTMGGLDFSV GFLVDTMTAM MMVVVTGVSL MVHIYTIGYM HDEKVGYQRF
FSYISLFTFS MLMLIMSNNF IQLFFGWEAV GLVSYLLIGF YFKRPSATFA NLKAFLINRV
GDFGFLLGIG LVLAYFGGSL RYQDVFAYLP NVQNATIQLF PGVEWSLITV TCLLLFVGAM
GKSAQFPLHV WLPDSMEGPT PISALIHAAT MVTAGLFMVS RMSPIYEMSS TALSVIMVIG
AITALFMGFL GVIQNDIKRV VAYSTLSQLG YMTVALGASA YSVAMFHVMT HAFFKALLFL
AAGSAIIGMH HDQDMRHMGN LKKYMPVTWL TMLIGNLSLI GTPFFSGFYS KDSIIEAAKY
STLPGSGFAY FAVLASVFVT AFYAFRQYFM VFHGEEKWRS LPEHHSDGHG EEHHGLGKND
NPHESPLVVT LPLILLAVPS VIIGYIAIEP MLYGDFFKDV IFVNADAHPT IHIMKEEFHG
ALAMVSHSLH SPVLYLAIAG VLSAWLLYVK LPHLPAKIAQ TFRPIYVLFE NKYYLDALYF
NVFAKGTRAL GTFFWKVGDT AIIDNGIVNG SAKLVGAIAA QVRKAQTGFI YTYAAAMVFG
VLVLLGMTFW GLFR
