TM175_MARTH
ID TM175_MARTH Reviewed; 247 AA.
AC E4TN31;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Potassium channel Ftrac_2467 {ECO:0000305};
DE AltName: Full=Transmembrane protein 175 {ECO:0000303|PubMed:32267231};
DE Short=MtTMEM175 {ECO:0000303|PubMed:32267231};
GN OrderedLocusNames=Ftrac_2467 {ECO:0000312|EMBL:ADR22445.1};
OS Marivirga tractuosa (strain ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB 1408
OS / VKM B-1430 / H-43) (Microscilla tractuosa) (Flexibacter tractuosus).
OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Marivirgaceae;
OC Marivirga.
OX NCBI_TaxID=643867;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB 1408 / VKM B-1430 / H-43
RC {ECO:0000312|Proteomes:UP000008720};
RX PubMed=21677852; DOI=10.4056/sigs.1623941;
RA Pagani I., Chertkov O., Lapidus A., Lucas S., Del Rio T.G., Tice H.,
RA Copeland A., Cheng J.F., Nolan M., Saunders E., Pitluck S., Held B.,
RA Goodwin L., Liolios K., Ovchinikova G., Ivanova N., Mavromatis K., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA Han C., Tapia R., Ngatchou-Djao O.D., Rohde M., Goker M., Spring S.,
RA Sikorski J., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Marivirga tractuosa type strain (H-43).";
RL Stand. Genomic Sci. 4:154-162(2011).
RN [2] {ECO:0007744|PDB:6HD8, ECO:0007744|PDB:6HD9, ECO:0007744|PDB:6HDA, ECO:0007744|PDB:6HDB, ECO:0007744|PDB:6HDC, ECO:0007744|PDB:6SWR}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-247, FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF THR-38.
RX PubMed=32267231; DOI=10.7554/elife.53683;
RA Brunner J.D., Jakob R.P., Schulze T., Neldner Y., Moroni A., Thiel G.,
RA Maier T., Schenck S.;
RT "Structural basis for ion selectivity in TMEM175 K+ channels.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: Potassium channel; forms a potassium-permeable leak-like
CC channel with weak selectivity for potassium (PubMed:32267231). The
CC channel is permeable for K(+), Rb(+) and Cs(+) (PubMed:32267231).
CC {ECO:0000269|PubMed:32267231}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:32267231}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:32267231};
CC Multi-pass membrane protein {ECO:0000269|PubMed:32267231}.
CC -!- DOMAIN: The six transmembrane regions are tightly packed within each
CC subunit without undergoing domain swapping (PubMed:32267231).
CC Transmembranes TM1-TM3 are positioned on the inner circle of the
CC channel tetramer and participate in inter-subunit interactions that are
CC central to the assembly of the ion conduction pore (PubMed:32267231).
CC The RxxxFSD motif within transmembrane TM1 coordinates a network of
CC specific inter- and intra-subunit interactions with other conserved
CC residues on TM2 and TM3 and plays a key role in the tetrameric assembly
CC of the channel (PubMed:32267231). Transmembrane TM4-TM6 are positioned
CC on the periphery of the channel and do not contribute to contacts with
CC neighboring subunits (By similarity). Transmembrane TM1 forms the pore-
CC lining inner helix at the center of the channel, creating an hourglass-
CC shaped ion permeation pathway in the channel tetramer (By similarity).
CC Hydrophobic residues (Leu-35, Leu-39 and Leu-42) on the C-terminal half
CC of the TM1 helix form a bottleneck along the ion conduction pathway and
CC serve as the selectivity filter of the channel (PubMed:32267231). Thr-
CC 38 is required for potassium ion selectivity (PubMed:32267231).
CC {ECO:0000250|UniProtKB:K9UJK2, ECO:0000269|PubMed:32267231}.
CC -!- SIMILARITY: Belongs to the TMEM175 family. {ECO:0000305}.
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DR EMBL; CP002349; ADR22445.1; -; Genomic_DNA.
DR RefSeq; WP_013454588.1; NC_014759.1.
DR PDB; 6HD8; X-ray; 2.40 A; B=2-247.
DR PDB; 6HD9; X-ray; 3.50 A; B=2-247.
DR PDB; 6HDA; X-ray; 3.80 A; B=2-247.
DR PDB; 6HDB; X-ray; 2.90 A; B=2-247.
DR PDB; 6HDC; X-ray; 3.40 A; B=2-247.
DR PDB; 6SWR; X-ray; 3.20 A; B/E=2-247.
DR PDBsum; 6HD8; -.
DR PDBsum; 6HD9; -.
DR PDBsum; 6HDA; -.
DR PDBsum; 6HDB; -.
DR PDBsum; 6HDC; -.
DR PDBsum; 6SWR; -.
DR AlphaFoldDB; E4TN31; -.
DR SMR; E4TN31; -.
DR STRING; 643867.Ftrac_2467; -.
DR EnsemblBacteria; ADR22445; ADR22445; Ftrac_2467.
DR KEGG; mtt:Ftrac_2467; -.
DR eggNOG; COG3548; Bacteria.
DR HOGENOM; CLU_093496_0_0_10; -.
DR OMA; HNEHEPV; -.
DR OrthoDB; 1909520at2; -.
DR Proteomes; UP000008720; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0022841; F:potassium ion leak channel activity; IDA:UniProtKB.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR InterPro; IPR010617; TMEM175.
DR Pfam; PF06736; TMEM175; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Ion channel; Ion transport; Membrane;
KW Potassium; Potassium channel; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..247
FT /note="Potassium channel Ftrac_2467"
FT /id="PRO_0000452678"
FT TRANSMEM 23..44
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:32267231,
FT ECO:0007744|PDB:6HD8, ECO:0007744|PDB:6HD9,
FT ECO:0007744|PDB:6HDA, ECO:0007744|PDB:6HDB,
FT ECO:0007744|PDB:6HDC, ECO:0007744|PDB:6SWR"
FT TRANSMEM 56..78
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:32267231,
FT ECO:0007744|PDB:6HD8, ECO:0007744|PDB:6HD9,
FT ECO:0007744|PDB:6HDA, ECO:0007744|PDB:6HDB,
FT ECO:0007744|PDB:6HDC, ECO:0007744|PDB:6SWR"
FT TRANSMEM 89..117
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:32267231,
FT ECO:0007744|PDB:6HD8, ECO:0007744|PDB:6HD9,
FT ECO:0007744|PDB:6HDA, ECO:0007744|PDB:6HDB,
FT ECO:0007744|PDB:6HDC, ECO:0007744|PDB:6SWR"
FT TRANSMEM 142..165
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:32267231,
FT ECO:0007744|PDB:6HD8, ECO:0007744|PDB:6HD9,
FT ECO:0007744|PDB:6HDA, ECO:0007744|PDB:6HDB,
FT ECO:0007744|PDB:6HDC, ECO:0007744|PDB:6SWR"
FT TRANSMEM 187..210
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:32267231,
FT ECO:0007744|PDB:6HD8, ECO:0007744|PDB:6HD9,
FT ECO:0007744|PDB:6HDA, ECO:0007744|PDB:6HDB,
FT ECO:0007744|PDB:6HDC, ECO:0007744|PDB:6SWR"
FT TRANSMEM 215..237
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:32267231,
FT ECO:0007744|PDB:6HD8, ECO:0007744|PDB:6HD9,
FT ECO:0007744|PDB:6HDA, ECO:0007744|PDB:6HDB,
FT ECO:0007744|PDB:6HDC, ECO:0007744|PDB:6SWR"
FT MOTIF 24..30
FT /note="RxxxFSD motif"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT SITE 35
FT /note="Hydrophobic filter residue 1"
FT /evidence="ECO:0000269|PubMed:32267231"
FT SITE 39
FT /note="Hydrophobic filter residue 2"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT SITE 42
FT /note="Hydrophobic filter residue 3"
FT /evidence="ECO:0000250|UniProtKB:K9UJK2"
FT MUTAGEN 38
FT /note="T->A: Decreased selectivity for potassium ion."
FT /evidence="ECO:0000269|PubMed:32267231"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:6HDB"
FT HELIX 24..42
FT /evidence="ECO:0007829|PDB:6HD8"
FT HELIX 50..58
FT /evidence="ECO:0007829|PDB:6HD8"
FT HELIX 60..84
FT /evidence="ECO:0007829|PDB:6HD8"
FT HELIX 89..124
FT /evidence="ECO:0007829|PDB:6HD8"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:6HD8"
FT HELIX 139..169
FT /evidence="ECO:0007829|PDB:6HD8"
FT TURN 170..175
FT /evidence="ECO:0007829|PDB:6HD8"
FT HELIX 178..207
FT /evidence="ECO:0007829|PDB:6HD8"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:6HD8"
FT HELIX 214..224
FT /evidence="ECO:0007829|PDB:6HD8"
FT HELIX 226..239
FT /evidence="ECO:0007829|PDB:6HD8"
SQ SEQUENCE 247 AA; 28569 MW; 2F02B4F056C23CCC CRC64;
MRKVFETVVG LNPNFSFRGK QQTRIETFSD AVFALAITLL VLSSTIPETF EDLWASMRDV
IPFAICVALI IVIWYQHYIF FLKYGLQDKV TILLNTILLF VLLVYVYPLK FLARFLSEIY
GGIFGIIETD LSRFGEYSHQ NLKLLMVNYG LGAFAIFLVF SLMYWRAYKM KSLLDLNSYE
IFDTKSSIIA NLLMCSVPLL SLIITLIDPW GNFRTTILSG FLYFLYVPIM IVFGRITSKK
SRRLLQD
