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NUOL_RICBR
ID   NUOL_RICBR              Reviewed;         642 AA.
AC   Q1RKE6;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=RBE_0087;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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; CP000087; ABE04168.1; -; Genomic_DNA.
DR   RefSeq; WP_011476783.1; NC_007940.1.
DR   AlphaFoldDB; Q1RKE6; -.
DR   SMR; Q1RKE6; -.
DR   STRING; 336407.RBE_0087; -.
DR   EnsemblBacteria; ABE04168; ABE04168; RBE_0087.
DR   KEGG; rbe:RBE_0087; -.
DR   eggNOG; COG1009; Bacteria.
DR   HOGENOM; CLU_007100_6_0_5; -.
DR   OMA; LIGFWQH; -.
DR   OrthoDB; 1274678at2; -.
DR   Proteomes; UP000001951; 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..642
FT                   /note="NADH-quinone oxidoreductase subunit L"
FT                   /id="PRO_0000287835"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        255..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        287..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        315..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        340..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        383..403
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        418..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        467..487
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        513..533
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        622..642
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   642 AA;  71911 MW;  EEB9B220C02E6A66 CRC64;
     MYKSIAIMII LLPLASALIN GLFVRRIDKK LASIVATSFL SLSALFALII FYHTGLNGHI
     IHIKLLPWIE VSQFKVDWSI YIDQLTSIMF IAVTWVSSVV HIYSLGYMSR DKGIVRFLSF
     LSLFTFFMLM LVSADNFLQL FFGWEGVGIC SYLLIGFWYS KESANKAAIK AFIANRVGDF
     AFILGVITII FYCHSANYED VFLLAPKLAN TKILLADFEI SILDIACLLL FIGCMGKSAQ
     IGLHVWLPDA MEGPTPVSAL IHAATMVTAG VFLVARCSYL FEYSPMVLQF ITIIGGITCL
     FAASIAIMQN DIKKIIAYST CSQLGYMFMA CGVSAYNSGI FHLVTHAFFK ALLFLSAGSV
     IHAVHEQDIF KMGELRNKMP ITYGNFLIGS LALIGIYPLA GFYSKDSILE AAYSSGSFMF
     IFGILAAILT AIYSMKIIML VFHGKTRLEK DVFEHAHEPP KVMNNPLTLL VAGSFFSGMI
     GYYLLSMDKP NGYFHDSLLN LHAYKLLITH PPLHIKLLPM VVGIIGIVVG IYLYKSDVVM
     SFLRRQESSK DNYFTKILIN KYYFDELYNF LIVKPINCLA CLFYSGDQKI IDRFGPNGFA
     RSVNCFSRLT GKTQTGYVFN YTLYVVLFVV VTISYFVWLV AV
 
 
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