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Database: UniProt
Entry: A0A085VIF1_PSESX
LinkDB: A0A085VIF1_PSESX
Original site: A0A085VIF1_PSESX 
ID   A0A085VIF1_PSESX        Unreviewed;       980 AA.
AC   A0A085VIF1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Monovalent cation/H+ antiporter subunit A {ECO:0000313|EMBL:KFE55214.1};
GN   ORFNames=IV01_13530 {ECO:0000313|EMBL:KFE55214.1};
OS   Pseudomonas syringae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=317 {ECO:0000313|EMBL:KFE55214.1, ECO:0000313|Proteomes:UP000028631};
RN   [1] {ECO:0000313|EMBL:KFE55214.1, ECO:0000313|Proteomes:UP000028631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GAW0119 {ECO:0000313|EMBL:KFE55214.1,
RC   ECO:0000313|Proteomes:UP000028631};
RA   Baltrus D.A., Berge O., Morris C.;
RT   "Draft Genome Sequences of Environmental Pseudomonas syringae strains.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KFE55214.1}.
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DR   EMBL; JPQU01000036; KFE55214.1; -; Genomic_DNA.
DR   RefSeq; WP_032628823.1; NZ_JPQU01000036.1.
DR   AlphaFoldDB; A0A085VIF1; -.
DR   PATRIC; fig|317.175.peg.2811; -.
DR   OrthoDB; 9811798at2; -.
DR   Proteomes; UP000028631; 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.
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   Signal {ECO:0000256|SAM:SignalP};
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   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..980
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001798922"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        108..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        133..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        242..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        270..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        367..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        409..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        459..482
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        502..523
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        574..596
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        602..624
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        631..651
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        657..679
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        700..721
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        759..777
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        814..841
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        847..867
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        888..907
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        927..949
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          64..110
FT                   /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00662"
FT   DOMAIN          126..407
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
FT   DOMAIN          615..680
FT                   /note="MrpA C-terminal/MbhD"
FT                   /evidence="ECO:0000259|Pfam:PF13244"
FT   DOMAIN          698..794
FT                   /note="MrpA C-terminal/MbhE"
FT                   /evidence="ECO:0000259|Pfam:PF20501"
FT   DOMAIN          821..943
FT                   /note="Na+/H+ antiporter MnhB subunit-related protein"
FT                   /evidence="ECO:0000259|Pfam:PF04039"
SQ   SEQUENCE   980 AA;  106461 MW;  2FFD422B14F12347 CRC64;
     MSLIVLLLLP FIGSCLAAFL PHNARNAESI LAGLVAVTGA IQVALWYPQI VDGGVIREEY
     FWLPSLGLNF VLRMDGFAWL FSMLVLGIGA LVALYARYYM SPDDPVPRFF AFFLAFMGAM
     LGLVISGNLI QMVFFWELTS VFSFLLIGYW HHRADARRGA YMALMVTGTG GLALLVGVML
     LGHVVGSYDL DRVLASGEAI RAHALYPVLL TLILIGALSK SAQFPFHFWL PHAMAAPTPV
     SAYLHSATMV KAGVFLLARF WPALSGTEQW FWMVSGAGAC TLIIGAYAAI FQNDLKGLLA
     YSTISHLGLI TLLLGLNSPL AAVAAVFHIL NHATFKASLF MAAGIIDHES GTRDIRKLSG
     LIKLMPYTAT LAMVASASMA GVPLLNGFLS KEMFFAETVF ISSSAWVEMA LPVIATIAGT
     FSVAYSLRFT ADVFFGPKAT DLPHTPHEPP RWMRAPVEFL VIACVIVGIF PAQSVAPLLA
     AAAQPVVGGM LPEYSLAVWH GWNAPMIMSL IAMAGGILLY LLLRQPFKQH RFAGPPLVNR
     LNGKRFFERS LILLTRWARR LERNISTGRL QPQLFLVVLA ALIGGFIPMY FSGLTWGDRP
     KIPGSGVFVT LWIIAIACAL GAAWQGKYHR LAAVIMVSVC GLMTCVTFVW FSAPDLALTQ
     LVVEVVTSVL ILLGLRWLPR RNEDVMPSVS TRLRARTRRV RDLILSILVG GGMALLSYAM
     LTRATPNTIS SFYLSRAIPE GGGSNVVNVM LVDFRGFDTF GEITVLAAVA LTVFALLRRF
     RPPKESIALP AQQRLLARDV VTDLVNPRSA SDTALGFMMV PAVLVRLLLP IAVVVSMYLF
     MRGHNQPGGG FVAGLVMSVA FILQYMVAGT QWVEAQMRLR PLRWMGTGLL FAIGTGLGSM
     FFGYPFMTTH TAHFALPVLG DIHVASALFF DVGVYAVVVG STLLILTALA HQSVRSHRPT
     SLPKPVPTPI AELMAEKGAS
//
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