NUOL_RICTY
ID NUOL_RICTY Reviewed; 653 AA.
AC Q68VV7;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=RT0779;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. Couples the redox
CC reaction to proton translocation (for every two electrons transferred,
CC four hydrogen ions are translocated across the cytoplasmic membrane),
CC and thus conserves the redox energy in a proton gradient (By
CC 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}.
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DR EMBL; AE017197; AAU04235.1; -; Genomic_DNA.
DR RefSeq; WP_011191210.1; NC_006142.1.
DR AlphaFoldDB; Q68VV7; -.
DR SMR; Q68VV7; -.
DR STRING; 257363.RT0779; -.
DR EnsemblBacteria; AAU04235; AAU04235; RT0779.
DR KEGG; rty:RT0779; -.
DR eggNOG; COG1009; Bacteria.
DR HOGENOM; CLU_007100_6_0_5; -.
DR OMA; LIGFWQH; -.
DR OrthoDB; 1274678at2; -.
DR Proteomes; UP000000604; 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 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; Translocase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..653
FT /note="NADH-quinone oxidoreductase subunit L"
FT /id="PRO_0000287837"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 577..597
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 629..649
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 653 AA; 73528 MW; C18D8E67CC297A67 CRC64;
MIHQNLAIMI IILPLVSSVI NGLFLNRIDK KLAKIIAISF LLLSALFSLI IFCDATLVGK
IIHIKLLPWI EFRNFKVNWS IYIDQLTSIM FIVVTFVSSV VHIYSLGYMA NDKGIIRFLS
FLSLFTFFML MLVSADNFLQ LFCGWEGVGV CSYLLIGFWY SKESANKAAM KAFITNRVSD
FAFILGIITI IIYNGSANYK DVFLSAKLLS NTKILVHFSI LDIICLLLSI GCIGKSAQIG
LHVWLPDAME GPTPVSALIH AATMVTAGIF LVARCSYLFE YSPIVLQFIT IIGGITCLFA
ASIAIMQSDI KKIIAYSTCS QLGYMFMACG VSSYNSAIFH LVTHAFFKAL LFLSAGSVIH
SVNEHNIFKM GNLINKMPIT YGNFLIGSLA LIGIYPLSGF YSKDLILEAA YSSGSFMFIF
GITAAMLTAI YSMKIIILVF HGKTKLEKDV FEHAHEPTKT MNNPLILLVA GSFFSGMLGY
YLLSMNKPNG YFHESLFNLH IYKLLINHTP LYIKLLPMAV GIVGIVIGIC LYKDSLPYHD
ALTNKSNKSK KDWIPQSNYK MILFIPNILR NKYYFDEIYN YLIIKPIHCL AYLFYLGDQK
IIDRFGPNGF ARVINYFCAL TCKIQTGYIF NYALYIVSFI VITISYFVWK SIY
