ID A0A074TDH4_9RHOB Unreviewed; 999 AA.
AC A0A074TDH4;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Monovalent cation/H+ antiporter subunit A {ECO:0000313|EMBL:KEP69821.1};
GN ORFNames=DL1_01990 {ECO:0000313|EMBL:KEP69821.1};
OS Thioclava dalianensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1185766 {ECO:0000313|EMBL:KEP69821.1, ECO:0000313|Proteomes:UP000027725};
RN [1] {ECO:0000313|EMBL:KEP69821.1, ECO:0000313|Proteomes:UP000027725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DLFJ1-1 {ECO:0000313|EMBL:KEP69821.1,
RC ECO:0000313|Proteomes:UP000027725};
RA Lai Q., Shao Z.;
RT "The draft genome sequence of Thioclava dalianensis DLFJ1-1.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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 ubiquinone. 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. {ECO:0000256|ARBA:ARBA00002378}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEP69821.1}.
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DR EMBL; JHEH01000010; KEP69821.1; -; Genomic_DNA.
DR RefSeq; WP_074854753.1; NZ_JHEH01000010.1.
DR AlphaFoldDB; A0A074TDH4; -.
DR STRING; 1185766.SAMN05216224_101676; -.
DR eggNOG; COG1009; Bacteria.
DR eggNOG; COG2111; Bacteria.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000027725; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR007182; MnhB.
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; PF04039; MnhB; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR Pfam; PF00662; Proton_antipo_N; 1.
DR PRINTS; PR01434; NADHDHGNASE5.
DR PRINTS; PR01435; NPOXDRDTASE5.
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 Reference proteome {ECO:0000313|Proteomes:UP000027725};
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 72..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 297..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 322..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 367..388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 408..429
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 450..477
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 497..521
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 564..583
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 595..617
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 624..644
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 650..672
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 684..706
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 749..770
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 791..812
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 818..839
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 851..876
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 896..921
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..108
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 126..403
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
FT DOMAIN 609..673
FT /note="MrpA C-terminal/MbhD"
FT /evidence="ECO:0000259|Pfam:PF13244"
FT DOMAIN 686..763
FT /note="MrpA C-terminal/MbhE"
FT /evidence="ECO:0000259|Pfam:PF20501"
FT DOMAIN 794..915
FT /note="Na+/H+ antiporter MnhB subunit-related protein"
FT /evidence="ECO:0000259|Pfam:PF04039"
FT REGION 980..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 999 AA; 107149 MW; 267242492CBB016B CRC64;
MSPALIAALP FLGAALPSLL IRTGRNNAAG VSAVITGLAL LGLLLHLPTT LAGGVVETRI
DWLPWLGLNL NFWIDGLGML FATMILGIGL LVILYARYYL SNKDPVGQFY TYLLLFQGAM
VGIVLSDNIL LLLVFWELTS LTSFLLIGYW KHLPAGRQGA RMALTVTGLG GLSMIAGMLI
LGQIAGSYDI SEILRHKDAI QASPLYIPAL LLILGGAFTK SAQFPFHFWL PHAMAAPTPV
SAYLHSATMV KAGLFLMARL WPVLSGTPEW FYIVSTVGLI TMLIAAYIAI FKHDMKALLA
FSTVSHLGLI TFMLGLGTQA GALAAVFHII NHATFKAALF MSAGIVDHEA GTRDLTRVGG
LRKLMPITFA ISTIAALSMA GIPFFNGFLS KEMMLEAAAH TVWLDNYWIV PAMATLAALL
SATYAFRFIH HAFFGEVATD LPKTPHDPPM GMWLSPAFLV VLVLAIGIFP MAVAGPYVQM
ATNAVVGGGY HMHPLKIWHG FTPALYMSAI AVLGGILFLT AHGPCQRVWD RMPRPEAKVM
FDWVVGRVQL GADRLTQGLY TGAMARYLML FALAAVGAGL YAFSTGSMGP QTRALTPVNG
AAVTAWILLL TATMCIVAFH HNRILALVLI SIVGLIVSIS FVYLSAPDLA MTQISVEVVT
AVLMLLALNF LPKVTKIESS RFKISFDVCI AVIGGVAVAG LIYALMTRDF AFPPMSGYML
ENSYNLAGGD NVVNVILVDF RGYDTYGEIT VLGIAALVIF ALTEALLQGA SSRKLIAWRP
DVARGGDKHP LLLLVATRVM MPIALVVGLF IFLRGHNLPG GGFIAGLIVA IALVMQYMAS
GFAWTQARQK VYYHVLIASG VLVAGITGAG AFFGGLPFLT SNFGYVKLPG LDKFELATAA
GFDLGVFLGV VGSVMLALGG LSRLARRAAM GEHDGEEGAH IAAEKPEARV LAPLSAGPYP
PEAKVPRRWW RTARAAREAT TAERDAVHAN KIKTQEEDH
//
