UMPB_HALZH
ID UMPB_HALZH Reviewed; 271 AA.
AC A0A1X9QDU5;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2017, sequence version 1.
DT 25-MAY-2022, entry version 8.
DE RecName: Full=Na(+), Li(+), K(+)/H(+) antiporter subunit B {ECO:0000305};
DE AltName: Full=Na(+) (Li(+)/K(+))/H(+) antiporter subunit B {ECO:0000305};
GN Name=umpB {ECO:0000303|PubMed:28652569};
OS Halomonas zhaodongensis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1176240;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=DSM 25869 / NEAU-ST10-25;
RX PubMed=28652569; DOI=10.1038/s41598-017-04236-0;
RA Meng L., Meng F., Zhang R., Zhang Z., Dong P., Sun K., Chen J., Zhang W.,
RA Yan M., Li J., Abdel-Motaal H., Jiang J.;
RT "Characterization of a novel two-component Na+(Li+, K+)/H+ antiporter from
RT Halomonas zhaodongensis.";
RL Sci. Rep. 7:4221-4221(2017).
CC -!- FUNCTION: Part of a two-component antiporter that catalyzes the efflux
CC of Na(+), Li(+) and K(+) in exchange for external protons. Shows a
CC preference for Na(+), followed by K(+) and Li(+).
CC {ECO:0000269|PubMed:28652569}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.0. Exhibits antiport activity at a wide pH range of
CC 6.5 to 9.5. {ECO:0000269|PubMed:28652569};
CC -!- SUBUNIT: Heterodimer composed of UmpA and UmpB.
CC {ECO:0000269|PubMed:28652569}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:28652569};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the UmpA/UmpB family. {ECO:0000305}.
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DR EMBL; KY241440; ARQ20735.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X9QDU5; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR011435; UmpAB.
DR Pfam; PF07556; DUF1538; 1.
PE 1: Evidence at protein level;
KW Antiport; Cell membrane; Ion transport; Membrane; Potassium;
KW Potassium transport; Sodium; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..271
FT /note="Na(+), Li(+), K(+)/H(+) antiporter subunit B"
FT /id="PRO_0000446279"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 252..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 271 AA; 29561 MW; FA89787D810997A5 CRC64;
MILLTIFWDT LLDILPIAAI IFGFQYIVIR KRIQRLPQVL AGFFMVWVGL SLFLVGLEQA
LFPMGELMAS QLTNTDFLPA VEQGVQRHWA DYYWVYLFAF AIGASTTIAE PSLIAVSIKA
GEISGGTINP FMLRIAVALG MAFGITLGTW RIVMGWPLQW FVFAAYCLVI IQTLRSPKSI
IPLAFDSGGV TTSTITVPII AALGLGLAAS IPGRSALMDG FGMIALACLF PIITVMGYAQ
IAQWKDKRKQ TTPHLSYSKA PPPSKGDNNA L