NUOL_RICPR
ID NUOL_RICPR Reviewed; 653 AA.
AC Q9ZCG1;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 100.
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=RP792;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
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}.
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; AJ235273; CAA15218.1; -; Genomic_DNA.
DR PIR; B71640; B71640.
DR RefSeq; NP_221142.1; NC_000963.1.
DR RefSeq; WP_004596922.1; NC_000963.1.
DR AlphaFoldDB; Q9ZCG1; -.
DR SMR; Q9ZCG1; -.
DR STRING; 272947.RP792; -.
DR EnsemblBacteria; CAA15218; CAA15218; CAA15218.
DR GeneID; 57569914; -.
DR KEGG; rpr:RP792; -.
DR PATRIC; fig|272947.5.peg.828; -.
DR eggNOG; COG1009; Bacteria.
DR HOGENOM; CLU_007100_6_0_5; -.
DR OMA; LIGFWQH; -.
DR Proteomes; UP000002480; 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; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..653
FT /note="NADH-quinone oxidoreductase subunit L"
FT /id="PRO_0000118223"
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; 73478 MW; 540436E913D097B4 CRC64;
MIHQNLAIMI IILPLVSSII NGLFLNIIDK KLAKIIAISF LSLSALFSLV IFCDVTLVGK
IIHIKLLPWI EFKNLQVNWS IYIDQLTSIM FIAVTFVSSV VHIYSLGYMA EDKGIIRFLS
FLSLFTFFML MLVSADNFLQ LFCGWEGVGV CSYLLIGFWH SKESANKAAI KAFITNRVSD
FAFILGIITI IVYYGSANYK DVFSSAKLLS NTKIFVHFSI LDIICLLLFI GCMGKSAQIG
LHVWLPDAME GPTPVSALIH AATMVTAGVF LVARCSYLFE YSPIVLQFIT IIGGITCLFA
ASIAIMQSDI KKIIAYSTCS QLGYMFMACG VSSYNSAIFH LVTHAFFKAL LFLSAGNVIH
AVNEHNIFKM GGLINKMPIT YGNFLIGSLA LIGIYPLSGF YSKDLILEAT YSSGSFMFIF
GIITAILTAI YSMKIIILVF HGKTKLEKDV FKHAHEPTKI MNNPLILLVA GSFFSGMIGY
YLLSMDKPNG YFHESLFNLH IYKLLINHHP LYIKLLPMAV GIVGIIIGIC LYKGSLSYQT
LTNESDQREK DWIPKSKCKM ILVFISNVLR NKYYFDEIYN HLIIKPIHCL TYLFYFGDQK
IIDRFGPNGF ARVINYFCAV TCKIQTGYIF NYTLYIVSFI VVTISYFVLK NIY
