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Database: UniProt
Entry: A0A1Q3VSK3_9PROT
LinkDB: A0A1Q3VSK3_9PROT
Original site: A0A1Q3VSK3_9PROT 
ID   A0A1Q3VSK3_9PROT        Unreviewed;        93 AA.
AC   A0A1Q3VSK3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=K+/H+ antiporter subunit F {ECO:0000313|EMBL:OJW49777.1};
GN   ORFNames=BGO63_18060 {ECO:0000313|EMBL:OJW49777.1};
OS   Candidatus Accumulibacter sp. 66-26.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=1895689 {ECO:0000313|EMBL:OJW49777.1, ECO:0000313|Proteomes:UP000186203};
RN   [1] {ECO:0000313|EMBL:OJW49777.1, ECO:0000313|Proteomes:UP000186203}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=66-26 {ECO:0000313|EMBL:OJW49777.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC       ECO:0000256|PIRNR:PIRNR028784}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|PIRNR:PIRNR028784}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the CPA3 antiporters (TC 2.A.63) subunit F
CC       family. {ECO:0000256|ARBA:ARBA00009212, ECO:0000256|PIRNR:PIRNR028784}.
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:OJW49777.1}.
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DR   EMBL; MKUH01000018; OJW49777.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3VSK3; -.
DR   STRING; 1895689.BGO63_18060; -.
DR   Proteomes; UP000186203; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015075; F:monoatomic ion transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   InterPro; IPR007208; MrpF/PhaF-like.
DR   PANTHER; PTHR34702:SF1; ANTIPORTER SUBUNIT MNHF2-RELATED; 1.
DR   PANTHER; PTHR34702; NA(+)/H(+) ANTIPORTER SUBUNIT F1; 1.
DR   Pfam; PF04066; MrpF_PhaF; 1.
DR   PIRSF; PIRSF028784; MrpF; 1.
PE   3: Inferred from homology;
KW   Antiport {ECO:0000256|PIRNR:PIRNR028784};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|PIRNR:PIRNR028784};
KW   Ion transport {ECO:0000256|PIRNR:PIRNR028784};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR028784};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR028784}.
FT   TRANSMEM        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        37..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        62..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   93 AA;  10103 MW;  AFA7A74A06D523D3 CRC64;
     MNAILPWAID FALLCFSLAM ICAVLRLLRG PTAQDRVLAL DTLYVNGMLT VLVLGIRLGS
     PVYFDIALLI AMFGFVGSAA MSKFLLRGEV IEP
//
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