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Database: UniProt
Entry: F0RJC1_DEIPM
LinkDB: F0RJC1_DEIPM
Original site: F0RJC1_DEIPM 
ID   F0RJC1_DEIPM            Unreviewed;       827 AA.
AC   F0RJC1;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=NADH dehydrogenase (Quinone) {ECO:0000313|EMBL:ADY25462.1};
DE            EC=1.6.99.5 {ECO:0000313|EMBL:ADY25462.1};
GN   OrderedLocusNames=Deipr_0289 {ECO:0000313|EMBL:ADY25462.1};
OS   Deinococcus proteolyticus (strain ATCC 35074 / DSM 20540 / JCM 6276 / NBRC
OS   101906 / NCIMB 13154 / VKM Ac-1939 / CCM 2703 / MRP).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=693977 {ECO:0000313|EMBL:ADY25462.1, ECO:0000313|Proteomes:UP000007718};
RN   [1] {ECO:0000313|Proteomes:UP000007718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 /
RC   VKM Ac-1939 / CCM 2703 / MRP {ECO:0000313|Proteomes:UP000007718};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G.,
RA   Zeytun A., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., Steenblock K.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete sequence of chromosome of Deinococcus proteolyticus DSM
RT   20540.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADY25462.1, ECO:0000313|Proteomes:UP000007718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 /
RC   VKM Ac-1939 / CCM 2703 / MRP {ECO:0000313|Proteomes:UP000007718};
RX   PubMed=22768367; DOI=10.4056/sigs.2756060;
RA   Copeland A., Zeytun A., Yassawong M., Nolan M., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S.,
RA   Mavromatis K., Liolios K., Pagani I., Ivanova N., Mikhailova N., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Brambilla E.M.,
RA   Rohde M., Sikorski J., Pukall R., Goker M., Detter J.C., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of the orange-red pigmented, radioresistant
RT   Deinococcus proteolyticus type strain (MRP(T)).";
RL   Stand. Genomic Sci. 6:240-250(2012).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU000320}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU000320}.
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DR   EMBL; CP002536; ADY25462.1; -; Genomic_DNA.
DR   RefSeq; WP_013614071.1; NC_015161.1.
DR   AlphaFoldDB; F0RJC1; -.
DR   STRING; 693977.Deipr_0289; -.
DR   KEGG; dpt:Deipr_0289; -.
DR   eggNOG; COG1009; Bacteria.
DR   eggNOG; COG2111; Bacteria.
DR   HOGENOM; CLU_007100_2_0_0; -.
DR   OrthoDB; 9807568at2; -.
DR   Proteomes; UP000007718; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR025383; MrpA_C/MbhD.
DR   InterPro; IPR046806; MrpA_C/MbhE.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   InterPro; IPR001516; Proton_antipo_N.
DR   PANTHER; PTHR43373:SF1; ANTIPORTER SUBUNIT MNHA2-RELATED; 1.
DR   PANTHER; PTHR43373; NA(+)/H(+) ANTIPORTER SUBUNIT; 1.
DR   Pfam; PF13244; MbhD; 1.
DR   Pfam; PF20501; MbhE; 1.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   Pfam; PF00662; Proton_antipo_N; 1.
DR   PRINTS; PR01434; NADHDHGNASE5.
PE   4: Predicted;
KW   Antiport {ECO:0000256|ARBA:ARBA00022449};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000313|EMBL:ADY25462.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007718};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000320};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        6..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        29..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        73..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        106..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        201..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        264..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        292..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        318..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        359..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        397..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        440..458
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        484..507
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        556..572
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        584..602
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        609..629
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        635..657
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        669..688
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        728..746
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          62..107
FT                   /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00662"
FT   DOMAIN          123..411
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
FT   DOMAIN          594..657
FT                   /note="MrpA C-terminal/MbhD"
FT                   /evidence="ECO:0000259|Pfam:PF13244"
FT   DOMAIN          671..752
FT                   /note="MrpA C-terminal/MbhE"
FT                   /evidence="ECO:0000259|Pfam:PF20501"
FT   REGION          783..827
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   827 AA;  89124 MW;  2B24040F6EC9F7A0 CRC64;
     MILAVFFPFL MAAVAAWAGL RLGRRTGYLA ALGFLPALLL ALPLSGMPAA APLREAIAWV
     PTLGLELGFR GDGFSLLFAV LIGVIGTLAS LYSVSYLSSN ERFARFYAYL LLFGGSMLGL
     VLSDNLIGLF GFWEMTSITS FLLIGLWHAR AAARDGAIKA FLVSALGGLA LLAAVAIIGT
     AGGSYNLSEI DLGALQASPL FIPAMLLTLL AAFTKSAQLP FHLWLPTAME APTPVSAFLH
     SATMVKAGVF LVAKFGLLFG GHPLWAAIIV PVGLATMTWG SYLALRQTDL KALLAFSTIS
     QLGLLMSLYG LADPEGRFAG TAHLLNHAAF KAALFFVVGI IDHETGTREI PQLGGLRRVF
     PVTFVLAVLA ALSMAGLPPL GGFISKELFF EAMIHHGLPF ILVAVVGSAL TIAYTVRFMS
     VWFGDLRHPG KERPERPTDA ILAPAALLVG AAVLFGLWPQ SVEELAGKAS AMLQFAEYHP
     HLSLWHGVTP ALVATLVTWA IAAFVWWRRD EFARIQQRLT PSWNANTMYY GFREWLDIVA
     TAVILRTQGL ALPSQLRWTL IAAFTLGGYA ILRAPPQFRL ELDVSFSLIL IVTLLVAGAI
     GVSLSRNRLT AVVLMGLTGF GSSAAFLAFR APDLALTQMI IETVTVILFL LAFRYMPGIR
     ALARTRTQYL VDLGIALSAG VGIMAYLLSV RPGLAESISP YYLQHSYTGG GGNNVVNVTL
     VDFRGFDTMG EITVVGMVGL AVLALLRLGK PGHAQPEYDT ADPTANMALI PTRQEREHIR
     QQLIESGTLS APQTLRTRRA ERRDQKNQQN QQSRGQSQGK RRKGGPQ
//
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