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NUOL_MYCTO
ID   NUOL_MYCTO              Reviewed;         633 AA.
AC   P9WIW0; L0TBP6; O86350;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 33.
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=MT3244;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK47583.1; -; Genomic_DNA.
DR   PIR; B70946; B70946.
DR   RefSeq; WP_003900642.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WIW0; -.
DR   SMR; P9WIW0; -.
DR   EnsemblBacteria; AAK47583; AAK47583; MT3244.
DR   KEGG; mtc:MT3244; -.
DR   PATRIC; fig|83331.31.peg.3492; -.
DR   HOGENOM; CLU_007100_6_0_11; -.
DR   Proteomes; UP000001020; 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..633
FT                   /note="NADH-quinone oxidoreductase subunit L"
FT                   /id="PRO_0000427936"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        188..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        284..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        322..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        382..402
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        412..432
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        468..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        505..525
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        613..633
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   633 AA;  66168 MW;  0ED0FC1C3F12FE3D CRC64;
     MTTSLGTHYT WLLVALPLAG AAILLFGGRR TDAWGHLLGC AAALAAFGVG AMLLADMLGR
     DGLERAIHQQ VFTWIPAGGL QVDFGLQIDQ LSMCFVLLIS GVGSLIHIYS VGYMAEDPDR
     RRFFGYLNLF LASMLLLVVA DNYVLLYVGW EGVGLASYLL IGFWYHKPSA ATAAKKAFVM
     NRVGDAGLAV GMFLTFSTFG TLSYAGVFAG VPAASRAVLT AIGLLMLLGA CAKSAQVPLQ
     AWLGDAMEGP TPVSALIHAA TMVTAGVYLI VRSGPLYNLA PTAQLAVVIV GAVTLLFGAI
     IGCAKDDIKR ALAASTISQI GYMVLAAGLG PAGYAFAIMH LLTHGFFKAG LFLGSGAVIH
     AMHEEQDMRR YGGLRAALPV TFATFGLAYL AIIGVPPFAG FFSKDAIIEA ALGAGGIRGS
     LLGGAALLGA GVTAFYMTRV MLMTFFGEKR WTPGAHPHEA PAVMTWPMIL LAVGSVFSGG
     LLAVGGTLRH WLQPVVGSHE EATHALPTWV ATTLALGVVA VGIAVAYRMY GTAPIPRVAP
     VRVSALTAAA RADLYGDAFN EEVFMRPGAQ LTNAVVAVDD AGVDGSVNAL ATLVSQTSNR
     LRQMQTGFAR NYALSMLVGA VLVAAALLVV QLW
 
 
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