TRKH_VIBPA
ID TRKH_VIBPA Reviewed; 485 AA.
AC Q87TN7;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Trk system potassium uptake protein TrkH {ECO:0000250|UniProtKB:P0AFZ7, ECO:0000312|EMBL:BAC58295.1};
GN Name=trkH {ECO:0000303|PubMed:21317882}; OrderedLocusNames=VP0032;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1] {ECO:0000312|EMBL:BAC58295.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
RN [2] {ECO:0000305, ECO:0000312|PDB:3PJZ}
RP X-RAY CRYSTALLOGRAPHY (3.51 ANGSTROMS) IN COMPLEX WITH POTASSIUM ION,
RP FUNCTION, SUBUNIT, TOPOLOGY, SELECTIVITY FILTER, AND MUTAGENESIS OF
RP ARG-468.
RX PubMed=21317882; DOI=10.1038/nature09731;
RA Cao Y., Jin X., Huang H., Derebe M.G., Levin E.J., Kabaleeswaran V.,
RA Pan Y., Punta M., Love J., Weng J., Quick M., Ye S., Kloss B., Bruni R.,
RA Martinez-Hackert E., Hendrickson W.A., Rost B., Javitch J.A.,
RA Rajashankar K.R., Jiang Y., Zhou M.;
RT "Crystal structure of a potassium ion transporter, TrkH.";
RL Nature 471:336-340(2011).
CC -!- FUNCTION: Low-affinity potassium transport system. Interacts with trk
CC system potassium uptake protein TrkA and requires TrkE for transport
CC activity. Selective for permeation of potassium ion and rubidium ion
CC over smaller ions such as natrium or litium.
CC {ECO:0000250|UniProtKB:P0AFZ7, ECO:0000269|PubMed:21317882}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21317882}.
CC -!- INTERACTION:
CC Q87TN7; Q87TN7: trkH; NbExp=4; IntAct=EBI-15912091, EBI-15912091;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P23849}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P23849, ECO:0000303|PubMed:21317882}.
CC -!- SIMILARITY: Belongs to the TrkH potassium transport family.
CC {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000031; BAC58295.1; -; Genomic_DNA.
DR RefSeq; NP_796411.1; NC_004603.1.
DR RefSeq; WP_005465049.1; NC_004603.1.
DR PDB; 3PJZ; X-ray; 3.51 A; A/B=1-485.
DR PDB; 4J9U; X-ray; 3.80 A; A/B/C/D=1-485.
DR PDB; 6V4J; EM; 2.97 A; A/B/C/D=1-485.
DR PDB; 6V4K; X-ray; 3.53 A; A/B/C/D=1-485.
DR PDB; 6V4L; X-ray; 3.80 A; A/B=1-485.
DR PDBsum; 3PJZ; -.
DR PDBsum; 4J9U; -.
DR PDBsum; 6V4J; -.
DR PDBsum; 6V4K; -.
DR PDBsum; 6V4L; -.
DR AlphaFoldDB; Q87TN7; -.
DR SMR; Q87TN7; -.
DR DIP; DIP-59200N; -.
DR STRING; 223926.28805014; -.
DR TCDB; 2.A.38.1.5; the k(+) transporter (trk) family.
DR EnsemblBacteria; BAC58295; BAC58295; BAC58295.
DR GeneID; 1187488; -.
DR KEGG; vpa:VP0032; -.
DR PATRIC; fig|223926.6.peg.32; -.
DR eggNOG; COG0168; Bacteria.
DR HOGENOM; CLU_030708_0_2_6; -.
DR OMA; LQWMGGM; -.
DR Proteomes; UP000002493; Chromosome 1.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005267; F:potassium channel activity; IDA:UniProtKB.
DR GO; GO:0030955; F:potassium ion binding; IDA:UniProtKB.
DR GO; GO:0015379; F:potassium:chloride symporter activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
DR InterPro; IPR003445; Cat_transpt.
DR InterPro; IPR004772; TrkH.
DR Pfam; PF02386; TrkH; 1.
DR PIRSF; PIRSF006247; TrkH; 1.
DR TIGRFAMs; TIGR00933; 2a38; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Ion channel;
KW Ion transport; Membrane; Metal-binding; Potassium; Potassium transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..485
FT /note="Trk system potassium uptake protein TrkH"
FT /id="PRO_0000419291"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21317882"
FT TRANSMEM 3..29
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21317882"
FT TOPO_DOM 30..35
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:21317882"
FT TRANSMEM 36..57
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21317882"
FT TOPO_DOM 58..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21317882"
FT TRANSMEM 66..90
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21317882"
FT TOPO_DOM 91..?
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:21317882"
FT INTRAMEM ?..97
FT /evidence="ECO:0000269|PubMed:21317882"
FT INTRAMEM 98..109
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000269|PubMed:21317882"
FT INTRAMEM 110..115
FT /evidence="ECO:0000269|PubMed:21317882"
FT TOPO_DOM 116..124
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:21317882"
FT TRANSMEM 125..150
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21317882"
FT TOPO_DOM 151..177
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21317882"
FT TRANSMEM 178..202
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21317882"
FT TOPO_DOM 203..205
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:21317882"
FT INTRAMEM 206
FT /evidence="ECO:0000269|PubMed:21317882"
FT INTRAMEM 207..218
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000269|PubMed:21317882"
FT INTRAMEM 219..224
FT /evidence="ECO:0000269|PubMed:21317882"
FT TOPO_DOM 225..234
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:21317882"
FT INTRAMEM 235..250
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21317882"
FT INTRAMEM 251..?
FT /evidence="ECO:0000269|PubMed:21317882"
FT TOPO_DOM ?..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21317882"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21317882"
FT TOPO_DOM 297..?
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:21317882"
FT INTRAMEM ?..302
FT /evidence="ECO:0000269|PubMed:21317882"
FT INTRAMEM 303..318
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000269|PubMed:21317882"
FT INTRAMEM 319..324
FT /evidence="ECO:0000269|PubMed:21317882"
FT TOPO_DOM 325..332
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:21317882"
FT INTRAMEM 333..344
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21317882"
FT INTRAMEM 345..357
FT /note="Note=Loop between two helices"
FT /evidence="ECO:0000269|PubMed:21317882"
FT INTRAMEM 358..?
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21317882"
FT TOPO_DOM ?..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21317882"
FT TRANSMEM 392..419
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21317882"
FT TOPO_DOM 420..421
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:21317882"
FT INTRAMEM 422..423
FT /evidence="ECO:0000269|PubMed:21317882"
FT INTRAMEM 424..434
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000269|PubMed:21317882"
FT INTRAMEM 435..441
FT /evidence="ECO:0000269|PubMed:21317882"
FT TOPO_DOM 442..453
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:21317882"
FT INTRAMEM 454..465
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21317882"
FT INTRAMEM 466..?
FT /evidence="ECO:0000269|PubMed:21317882"
FT TOPO_DOM ?..485
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21317882"
FT REGION 110..115
FT /note="Selectivity filter part 1"
FT /evidence="ECO:0000305"
FT REGION 219..224
FT /note="Selectivity filter part 2"
FT /evidence="ECO:0000305"
FT REGION 319..324
FT /note="Selectivity filter part 3"
FT /evidence="ECO:0000305"
FT REGION 436..441
FT /note="Selectivity filter part 4"
FT /evidence="ECO:0000305"
FT BINDING 111
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:21317882"
FT BINDING 112
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:21317882"
FT BINDING 220
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:21317882"
FT BINDING 221
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:21317882"
FT BINDING 320
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:21317882"
FT BINDING 321
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:21317882"
FT BINDING 437
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:21317882"
FT BINDING 438
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:21317882"
FT MUTAGEN 468
FT /note="R->A: Significant increase in the rate of potassium
FT ion flux."
FT /evidence="ECO:0000269|PubMed:21317882"
FT HELIX 3..19
FT /evidence="ECO:0007829|PDB:6V4J"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:6V4J"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:6V4J"
FT TURN 48..54
FT /evidence="ECO:0007829|PDB:6V4J"
FT HELIX 70..75
FT /evidence="ECO:0007829|PDB:6V4J"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:6V4J"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:6V4J"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:6V4J"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:6V4J"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:6V4J"
FT HELIX 125..148
FT /evidence="ECO:0007829|PDB:6V4J"
FT TURN 149..152
FT /evidence="ECO:0007829|PDB:6V4J"
FT HELIX 181..201
FT /evidence="ECO:0007829|PDB:6V4J"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:6V4J"
FT HELIX 207..216
FT /evidence="ECO:0007829|PDB:6V4J"
FT STRAND 225..233
FT /evidence="ECO:0007829|PDB:6V4J"
FT HELIX 236..251
FT /evidence="ECO:0007829|PDB:6V4J"
FT HELIX 255..260
FT /evidence="ECO:0007829|PDB:6V4J"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:6V4J"
FT HELIX 266..270
FT /evidence="ECO:0007829|PDB:6V4J"
FT HELIX 274..297
FT /evidence="ECO:0007829|PDB:6V4J"
FT HELIX 303..318
FT /evidence="ECO:0007829|PDB:6V4J"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:6V4J"
FT HELIX 334..344
FT /evidence="ECO:0007829|PDB:6V4J"
FT HELIX 358..376
FT /evidence="ECO:0007829|PDB:6V4J"
FT HELIX 393..419
FT /evidence="ECO:0007829|PDB:6V4J"
FT HELIX 425..434
FT /evidence="ECO:0007829|PDB:6V4J"
FT TURN 435..437
FT /evidence="ECO:0007829|PDB:6V4J"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:6V4J"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:6V4J"
FT HELIX 454..468
FT /evidence="ECO:0007829|PDB:6V4J"
FT HELIX 472..478
FT /evidence="ECO:0007829|PDB:6V4J"
FT TURN 480..482
FT /evidence="ECO:0007829|PDB:6V4J"
SQ SEQUENCE 485 AA; 53064 MW; B92893EAF3764EB2 CRC64;
MQFRSIIRIV GLLLALFSVT MLAPALVALL YRDGAGVPFV TTFFVLLFCG AMCWFPNRRH
KHELKSRDGF LIVVLFWTVL GSAGSLPFLI ADNPNISVTD AFFESFSALT TTGATVIVGL
DELPKAILFY RQFLQWFGGM GIIVLAVAIL PVLGIGGMQL YRAEIPGPVK DTKMTPRIAE
TAKALWYIYL SLTIACAVAF WLAGMTPFDA ISHSFSTIAI GGFSTHDASM GYFDSYAINL
ITVVFLLISA CNFTLHFAAF ASGGVHPKYY WKDPEFRAFI FIQVLLFLVC FLLLLKHHSY
TSPYDAFDQA LFQTVSISTT AGFTTTGFAD WPLFLPVLLL FSSFIGGCAG STGGGMKVIR
ILLLTLQGAR ELKRLVHPRA VYTIKVGGSA LPQRVVDAVW GFFSAYALVF VVCMLGLIAT
GMDELSAFSA VAATLNNLGP GLGEVALHFG DVNDKAKWVL IVSMLFGRLE IFTLLILLTP
TFWRS
