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Database: UniProt
Entry: D1A459_THECD
LinkDB: D1A459_THECD
Original site: D1A459_THECD 
ID   D1A459_THECD            Unreviewed;       516 AA.
AC   D1A459;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Proton-translocating NADH-quinone oxidoreductase, chain M {ECO:0000313|EMBL:ACY99933.1};
DE            EC=1.6.99.5 {ECO:0000313|EMBL:ACY99933.1};
GN   OrderedLocusNames=Tcur_4406 {ECO:0000313|EMBL:ACY99933.1};
OS   Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC
OS   9072 / NBRC 15933 / NCIMB 10081 / Henssen B9).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Thermomonospora.
OX   NCBI_TaxID=471852 {ECO:0000313|EMBL:ACY99933.1, ECO:0000313|Proteomes:UP000001918};
RN   [1] {ECO:0000313|EMBL:ACY99933.1, ECO:0000313|Proteomes:UP000001918}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 /
RC   NCIMB 10081 / Henssen B9 {ECO:0000313|Proteomes:UP000001918};
RX   PubMed=21475583; DOI=10.4056/sigs.1453580;
RA   Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., Del Rio T.G.,
RA   Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Brettin T., Han C., Detter J.C., Rohde M., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Thermomonospora curvata type strain (B9).";
RL   Stand. Genomic Sci. 1:13-22(2011).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU000320}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU000320}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 4 family.
CC       {ECO:0000256|ARBA:ARBA00009025}.
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DR   EMBL; CP001738; ACY99933.1; -; Genomic_DNA.
DR   RefSeq; WP_012854716.1; NC_013510.1.
DR   AlphaFoldDB; D1A459; -.
DR   STRING; 471852.Tcur_4406; -.
DR   KEGG; tcu:Tcur_4406; -.
DR   eggNOG; COG1008; Bacteria.
DR   HOGENOM; CLU_007100_4_4_11; -.
DR   OrthoDB; 9768329at2; -.
DR   Proteomes; UP000001918; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   InterPro; IPR010227; NADH_Q_OxRdtase_chainM/4.
DR   InterPro; IPR003918; NADH_UbQ_OxRdtase.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   NCBIfam; TIGR01972; NDH_I_M; 1.
DR   PANTHER; PTHR43507:SF1; NAD(P)H-QUINONE OXIDOREDUCTASE CHAIN 4, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43507; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 4; 1.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   PRINTS; PR01437; NUOXDRDTASE4.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000313|EMBL:ACY99933.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001918};
KW   Transmembrane {ECO:0000256|RuleBase:RU000320, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        36..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        74..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        125..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        221..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        258..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        287..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        316..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        343..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        378..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        420..442
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        463..481
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          145..431
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
SQ   SEQUENCE   516 AA;  54822 MW;  2435BD0A2F0C3778 CRC64;
     MNDFPWLSVL IALPALGALG VALLPRGRDA LAKQVALGVS VLVAALAFVM AAGFEVGGPR
     HQFEEVYEWI PAFGVHWALG VDGVALVLIL MSVVLVPLVI VASWGEADRY GGVVAEGERP
     PAKSVKTYFA LILALEAMMV GVFAATDVFL FYIFFEVMLV PVYFLIGIFG GPQRSYAAVK
     FLLYSLLGGL LMLVAVIALY VQGPNTFLMS ELQGLKLDPA VAKWLFLGFF IAFAIKAPMV
     PVHTWLPDTA AQAPAGALVL IVGVLDKVGT YGMLRFCLEL FPEASKWAAP GVLTFAVISV
     IYGAVLAIGQ VDLKRLIAYT SISHFGFIVL GIFAMTSQGQ SGAALYMVNH GFSTGALFLI
     VGFLIVRRGS ARVDAFGGVQ KVAPLLAGAF LIAGLSGLSL PGLAPFVSEF LVLVGTFSRY
     QVAAVIAALG IVLAAVYILW MYQRTMNGPT AEAVAGFKDL SRRELTAIAP ILAIIVALGF
     FPKPVLDVID PSVQQTLRQV QVSDPTPTVA EKGARP
//
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