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Database: UniProt
Entry: F2RIP6_STRVP
LinkDB: F2RIP6_STRVP
Original site: F2RIP6_STRVP 
ID   F2RIP6_STRVP            Unreviewed;       525 AA.
AC   F2RIP6;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=NADH-ubiquinone oxidoreductase chain M {ECO:0000313|EMBL:CCA57602.1};
DE            EC=1.6.5.3 {ECO:0000313|EMBL:CCA57602.1};
GN   OrderedLocusNames=SVEN_4316 {ECO:0000313|EMBL:CCA57602.1};
OS   Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS   4526 / NBRC 13096 / PD 04745).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA57602.1, ECO:0000313|Proteomes:UP000006854};
RN   [1] {ECO:0000313|EMBL:CCA57602.1, ECO:0000313|Proteomes:UP000006854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 /
RC   PD 04745 {ECO:0000313|Proteomes:UP000006854};
RX   PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA   Pullan S.T., Bibb M.J., Merrick M.;
RT   "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT   provides new insights into global nitrogen regulation in actinomycetes.";
RL   BMC Genomics 12:175-175(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; FR845719; CCA57602.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2RIP6; -.
DR   STRING; 953739.SVEN_4316; -.
DR   KEGG; sve:SVEN_4316; -.
DR   PATRIC; fig|953739.5.peg.6817; -.
DR   eggNOG; COG1008; Bacteria.
DR   HOGENOM; CLU_007100_4_0_11; -.
DR   Proteomes; UP000006854; 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:CCA57602.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006854};
KW   Transmembrane {ECO:0000256|RuleBase:RU000320, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Ubiquinone {ECO:0000313|EMBL:CCA57602.1}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        43..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        153..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        182..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        220..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        259..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        291..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        325..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        351..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        400..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        441..464
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          148..432
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
SQ   SEQUENCE   525 AA;  54299 MW;  75F0685C1FB783A6 CRC64;
     MIDISESVMQ FLLALIVAGP LVGAAAALLP APPGLKGTSP DQAVLRHGVV VTGVILLAAI
     VLAVGFDHDQ PSTMQATTDI TWIKALDVRI HLGVDGISLP LLVLTALLTF LCALYSYFKM
     PAGPSPKGFV ALLLVLESGT LATFAVLDLV LFFLAFEMVL IPMYFLIARW GGEGKQAAAW
     KFILYTLLGS VVMLLGLLLI GVKAGTFDMV ALATDNGRGL TTSVQVIAVL AIGIGLAVKT
     PMWPLHSWLP DAHTAAPTVG SVLLAGVLLK MGTYGFVRIV LPIAPDGMRT FAPSLAAFAV
     AGIIYGSLAC LALARPGNKG DLKRLIAYSS VGHMGFVLLG IATMTPTGVN GALFANVAHG
     LVTGLLFFLV GAVKDRYGTA DLDTLAGATG AALYGRAPRL GALLAFAAVA SLGLPGLAGF
     WGEMLALFGA FDPAEGLSRP AFLTFMAIGA FGTLLTAAYL LLVVRRVCMG GPRPAGETPI
     ADVQGYEFAA WTPLVALTVL AGLWPAVLLG LTDPAVQKLL AGGTQ
//
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