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NUOL_RICFE
ID   NUOL_RICFE              Reviewed;         645 AA.
AC   Q4UK27;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=RF_1257;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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; CP000053; AAY62108.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4UK27; -.
DR   SMR; Q4UK27; -.
DR   STRING; 315456.RF_1257; -.
DR   EnsemblBacteria; AAY62108; AAY62108; RF_1257.
DR   KEGG; rfe:RF_1257; -.
DR   eggNOG; COG1009; Bacteria.
DR   HOGENOM; CLU_007100_6_0_5; -.
DR   OMA; LIGFWQH; -.
DR   Proteomes; UP000008548; 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..645
FT                   /note="NADH-quinone oxidoreductase subunit L"
FT                   /id="PRO_0000287836"
FT   TRANSMEM        7..27
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        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        284..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        312..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        337..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        415..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        464..484
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        510..530
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        623..643
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   645 AA;  71709 MW;  7249C256CB6358D3 CRC64;
     MYQNLAIMII MLPLASSVIN GLFLKVIDTK LAQIIATGFL SLSALFSLVI FCDAGLDGNI
     IHIKLLPWIE VGNFKVNWSI YIDQLTSIMF IAVTWVSSVV HIYSLGYMAE DKGIIRFLSF
     LSLFTFFMLM LVSADNFLQL FFGWEGVGVC SYLLIGFWYS KESANKAAIK AFITNRASDF
     AFILGIITII VYCGSANYKD VFSSAELLSN TKIFLQFSIL DVICLLLFIG CMGKSAQIGL
     HVWLPDAMEG PTPVSALIHA ATMVTAGVFL VARCSYLFEY SPLVLQFITI IGGVTCLFAA
     SIAIMQSDIK KIIAYSTCSQ LGYMFMACGV SAYNSGIFHL VTHAFFKALL FLSAGSIIHA
     VHEQDIFKMG DLRNKMPVTY GNSLIGSLAL IGIYPLAGFY SKDSILEAAY SSGSFMFIFG
     IAAAILTAIY SMKIIMLVFY GKTKLEKDVF EHAHEPAKIM NTPLILLVAG SFFSGMIGYY
     LLSMDKPNGY FHESLFNLHI YKLLISHPPL YIKLLPMAVG IMGIVIGICV YNSSTIMSFR
     PSSMSFPRKR ESSKPFNLVY NILHNKYYFD EIYNFLIVKP INCLASLFYL GDQKIIDRFG
     PNGFSRVVNC FSVLTGKTQT GYVFNYALYI VSFIVVVISV FVWKG
 
 
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