NUOL_MYCTU
ID NUOL_MYCTU Reviewed; 633 AA.
AC P9WIW1; L0TBP6; O86350;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 35.
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=Rv3156; ORFNames=MTCY03A2.02c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; AL123456; CCP45967.1; -; Genomic_DNA.
DR PIR; B70946; B70946.
DR RefSeq; NP_217672.1; NC_000962.3.
DR RefSeq; WP_003900642.1; NZ_NVQJ01000019.1.
DR AlphaFoldDB; P9WIW1; -.
DR SMR; P9WIW1; -.
DR STRING; 83332.Rv3156; -.
DR PaxDb; P9WIW1; -.
DR DNASU; 888063; -.
DR GeneID; 888063; -.
DR KEGG; mtu:Rv3156; -.
DR TubercuList; Rv3156; -.
DR eggNOG; COG1009; Bacteria.
DR OMA; LIGFWQH; -.
DR PhylomeDB; P9WIW1; -.
DR Proteomes; UP000001584; 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:0003954; F:NADH dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR GO; GO:0052572; P:response to host immune response; IMP:MTBBASE.
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 1: Evidence at protein level;
KW Cell membrane; Membrane; NAD; Quinone; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..633
FT /note="NADH-quinone oxidoreductase subunit L"
FT /id="PRO_0000118218"
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
