NUOL_CAMJE
ID NUOL_CAMJE Reviewed; 596 AA.
AC Q9PMA7; Q0P860;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=Cj1568c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(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 menaquinone. 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}.
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DR EMBL; AL111168; CAL35665.1; -; Genomic_DNA.
DR PIR; F81251; F81251.
DR RefSeq; WP_002851310.1; NC_002163.1.
DR RefSeq; YP_002344937.1; NC_002163.1.
DR AlphaFoldDB; Q9PMA7; -.
DR SMR; Q9PMA7; -.
DR IntAct; Q9PMA7; 10.
DR STRING; 192222.Cj1568c; -.
DR TCDB; 3.D.1.7.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; Q9PMA7; -.
DR PRIDE; Q9PMA7; -.
DR EnsemblBacteria; CAL35665; CAL35665; Cj1568c.
DR GeneID; 905250; -.
DR KEGG; cje:Cj1568c; -.
DR PATRIC; fig|192222.6.peg.1544; -.
DR eggNOG; COG1009; Bacteria.
DR HOGENOM; CLU_007100_6_0_7; -.
DR OMA; LIGFWQH; -.
DR Proteomes; UP000000799; 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..596
FT /note="NADH-quinone oxidoreductase subunit L"
FT /id="PRO_0000118217"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 480..500
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 576..596
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 596 AA; 66528 MW; 5296F1C1F21CF514 CRC64;
MQNLALISLF SPFVAFLFAS CFALSEKKQF VGIICSLLVA LSAFCSLYLL FCNEAFNVSL
FEWFAGVNFG FDIDAISLTM MSVVGIVATC VHFYSIFYMA HDEGFNKFFA YLGLFVFSML
FLVMSDNFLG LFVGWEGVGL CSWLLIGFWY KNDTYSFAAN EAFIMNRIAD LGMLLGIFWL
YLQAGTLKYD EVFSMAQSLD HNALILIATC LFIGAMGKSA QFPFHTWLAD AMAGPTPVSA
LIHAATMVTA GVYLVIRAST LYDLVPEVSY IIALLGAFVA IFAASMALVV RDLKRIIAYS
TLSQLGYMFV AAGLGAYGIA LFHLATHAFF KSLLFLGAGN VMHAMNDKLD IKKMGGLFKP
LKITAILMCI GSLALAGIYP FAGFFSKDLI LGYSFISFHH GIFLVLLIAA FLTAFYSFRL
LMLVFFTPAR HDEHPHEASK IALLAMSPLM VLAIIAGFFE HSFFEYLSTK LVFIDAQNQI
VMICASVAAI LGAILAIFAY KNSWFKESIE ENKIHKLLSN DYFIPQFYHQ FIVSKYESLC
AILKHCDLYI FDRIVEKIAL YSQNISQKMI MPNSLNLMLR FLVAAFVILL ILVWMV
