ID   HOXN_CUPNH              Reviewed;         351 AA.
AC   P23516;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2001, sequence version 3.
DT   25-MAY-2022, entry version 131.
DE   RecName: Full=High-affinity nickel transport protein;
GN   Name=hoxN; OrderedLocusNames=PHG023;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OG   Plasmid megaplasmid pHG1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1847142; DOI=10.1016/s0021-9258(18)49977-2;
RA   Eitinger T., Friedrich B.;
RT   "Cloning, nucleotide sequence, and heterologous expression of a high-
RT   affinity nickel transport gene from Alcaligenes eutrophus.";
RL   J. Biol. Chem. 266:3222-3227(1991).
RN   [2]
RP   SEQUENCE REVISION TO C-TERMINUS, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=7896709; DOI=10.1128/jb.177.7.1840-1843.1995;
RA   Wolfram L., Friedrich B., Eitinger T.;
RT   "The Alcaligenes eutrophus protein HoxN mediates nickel transport in
RT   Escherichia coli.";
RL   J. Bacteriol. 177:1840-1843(1995).
RN   [3]
RP   SEQUENCE REVISION TO 121.
RA   Eitinger T., Degen O.;
RT   "Ralstonia eutropha IS5-like insertion element IS881 containing a group II
RT   intron.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX   PubMed=12948488; DOI=10.1016/s0022-2836(03)00894-5;
RA   Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.;
RT   "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid
RT   encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis.";
RL   J. Mol. Biol. 332:369-383(2003).
RN   [5]
RP   SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=7934894; DOI=10.1111/j.1365-2958.1994.tb01090.x;
RA   Eitinger T., Friedrich B.;
RT   "A topological model for the high-affinity nickel transporter of
RT   Alcaligenes eutrophus.";
RL   Mol. Microbiol. 12:1025-1032(1994).
RN   [6]
RP   FUNCTION.
RX   PubMed=10201093; DOI=10.1007/s002030050691;
RA   Degen O., Kobayashi M., Shimizu S., Eitinger T.;
RT   "Selective transport of divalent cations by transition metal permeases: the
RT   Alcaligenes eutrophus HoxN and the Rhodococcus rhodochrous NhlF.";
RL   Arch. Microbiol. 171:139-145(1999).
CC   -!- FUNCTION: High-affinity nickel transporter responsible for nickel
CC       uptake. Necessary for high levels of activity of hydrogenase and
CC       urease. Does not transport cobalt. {ECO:0000269|PubMed:10201093,
CC       ECO:0000269|PubMed:7896709}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:7896709,
CC       ECO:0000269|PubMed:7934894}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:7896709, ECO:0000269|PubMed:7934894}.
CC   -!- SIMILARITY: Belongs to the NiCoT transporter (TC 2.A.52) family.
CC       {ECO:0000305}.
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DR   EMBL; AF261712; AAA69017.2; -; Genomic_DNA.
DR   EMBL; AY305378; AAP85779.1; -; Genomic_DNA.
DR   PIR; A39512; A39512.
DR   RefSeq; WP_011153948.1; NZ_CP039289.1.
DR   AlphaFoldDB; P23516; -.
DR   STRING; 381666.PHG023; -.
DR   TCDB; 2.A.52.1.1; the ni(2+)-co(2+) transporter (nicot) family.
DR   EnsemblBacteria; AAP85779; AAP85779; PHG023.
DR   GeneID; 39976657; -.
DR   KEGG; reh:PHG023; -.
DR   PATRIC; fig|381666.6.peg.18; -.
DR   eggNOG; COG3376; Bacteria.
DR   HOGENOM; CLU_036094_2_0_4; -.
DR   OMA; NGWVLYK; -.
DR   OrthoDB; 1515392at2; -.
DR   Proteomes; UP000008210; Plasmid megaplasmid pHG1.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0015099; F:nickel cation transmembrane transporter activity; IEA:InterPro.
DR   InterPro; IPR004688; Ni/Co_transpt.
DR   InterPro; IPR011541; Ni/Co_transpt_high_affinity.
DR   PANTHER; PTHR31611; PTHR31611; 1.
DR   Pfam; PF03824; NicO; 1.
DR   TIGRFAMs; TIGR00802; nico; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Ion transport; Membrane; Nickel;
KW   Nickel transport; Plasmid; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..351
FT                   /note="High-affinity nickel transport protein"
FT                   /id="PRO_0000194004"
FT   TOPO_DOM        1..19
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:7934894"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        41..51
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305|PubMed:7934894"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        73..94
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:7934894"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        116..128
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305|PubMed:7934894"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        150..199
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:7934894"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        221..243
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305|PubMed:7934894"
FT   TRANSMEM        244..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        265..269
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:7934894"
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        291..316
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305|PubMed:7934894"
FT   TRANSMEM        317..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        338..351
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:7934894"
SQ   SEQUENCE   351 AA;  38771 MW;  7787D9C05B69F19F CRC64;
     MFQLLAGVRM NSTGRPRAKI ILLYALLIAF NIGAWLCALA AFRDHPVLLG TALLAYGLGL
     RHAVDADHLA AIDNVTRKLM QDGRRPITAG LWFSLGHSSV VVLASVLIAV MATTLQERLD
     AFHEVGSVIG TLASALFLFA IAAINLVILR SAYRAFRRVR RGGIYVEEDF DLLFGNRGFL
     ARIFRPLFRF ITRSWHMYPL GMLFALGFDT ATEVALLGIS TMEASRGVPI WSILVFPALF
     TAGMALIDTI DSILMCGAYA WAYAKPVRKL YYNMTITFVS AIVALIVGGI ETLGLLADKF
     MLKGVFWNAV GALNENFCQL GFVIIGIFTV CWVVSIVVYR LRRYDDSEVR A