ID   NHLF_RHORH              Reviewed;         352 AA.
AC   P96454;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Cobalt transport protein NhlF;
GN   Name=nhlF;
OS   Rhodococcus rhodochrous.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=1829;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND ACTIVITY REGULATION.
RC   STRAIN=J1;
RX   PubMed=8990157; DOI=10.1073/pnas.94.1.36;
RA   Komeda H., Kobayashi M., Shimizu S.;
RT   "A novel transporter involved in cobalt uptake.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:36-41(1997).
RN   [2]
RP   FUNCTION AS A COBALT AND NICKEL IONS TRANSPORTER.
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: Mediates energy-dependent uptake of cobalt ions into the
CC       cell. Can also transport nickel ions, but cobalt is the preferred
CC       substrate. {ECO:0000269|PubMed:10201093, ECO:0000269|PubMed:8990157}.
CC   -!- ACTIVITY REGULATION: Cobalt uptake is inhibited by uncouplers (CCCP and
CC       3,5-di-tert-butyl-4-hydroxybenzylidenemalononitrile) and by the
CC       addition of excess nickel. {ECO:0000269|PubMed:8990157}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the NiCoT transporter (TC 2.A.52) family.
CC       {ECO:0000305}.
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DR   EMBL; D83695; BAA12063.1; -; Genomic_DNA.
DR   AlphaFoldDB; P96454; -.
DR   TCDB; 2.A.52.1.2; the ni(2+)-co(2+) transporter (nicot) family.
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   GO; GO:0006824; P:cobalt ion transport; IEA:UniProtKB-KW.
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 membrane; Cobalt; Cobalt transport; Ion transport; Membrane; Nickel;
KW   Nickel transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..352
FT                   /note="Cobalt transport protein NhlF"
FT                   /id="PRO_0000430351"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        323..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   352 AA;  37187 MW;  5512BAEA15C6F979 CRC64;
     MTSTTITPHH IGGAWTRTER RRLASVVGAI VILHVLGVAL YLGYSGNPAA AGGLAGSGVL
     AYVLGVRHAF DADHIAAIDD TTRLMLLRGR RPVGVGFFFA MGHSTVVVVL ALVVALGASA
     LTTTELEGVQ EIGGLVATVV AVTFLSIVAG LNSVVLRNLL CLSRQVRAGS DITGDLESRL
     SERGLFTRLL GNRWRGLVRS SWHMYPVGLL MGLGLETASE VTLLTLTASA ATGGTLSIAA
     VLSLPLLFAA GMSTFDTADS LFMTRAYSWS YQDPQRRLNF NIATTGATVV IGLFVAGIYV
     CALLAHLPMF AALSPIGDIS ENFEFLGYAV AAAFILTWTG ALLFNHLKPQ RN