NIXA_HELPY
ID NIXA_HELPY Reviewed; 331 AA.
AC Q48262;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=High-affinity nickel-transport protein NixA;
GN Name=nixA; OrderedLocusNames=HP_1077;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-331.
RC STRAIN=ATCC 43504;
RX PubMed=7651142; DOI=10.1111/j.1365-2958.1995.tb02395.x;
RA Mobley H.L.T., Garner R.M., Bauerfeind P.;
RT "Helicobacter pylori nickel-transport gene nixA: synthesis of catalytically
RT active urease in Escherichia coli independent of growth conditions.";
RL Mol. Microbiol. 16:97-109(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [3]
RP TOPOLOGY.
RX PubMed=10692379; DOI=10.1128/jb.182.6.1722-1730.2000;
RA Fulkerson J.F. Jr., Mobley H.L.;
RT "Membrane topology of the NixA nickel transporter of Helicobacter pylori:
RT two nickel transport-specific motifs within transmembrane helices II and
RT III.";
RL J. Bacteriol. 182:1722-1730(2000).
CC -!- FUNCTION: High-affinity nickel intake protein. Imports nickel ions in
CC an energy-dependent fashion. Necessary for the expression of
CC catalytically active urease.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NiCoT transporter (TC 2.A.52) family.
CC {ECO:0000305}.
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DR EMBL; Z48742; CAA88633.1; -; Genomic_DNA.
DR EMBL; AE000511; AAD08119.1; -; Genomic_DNA.
DR PIR; E64654; S53113.
DR RefSeq; NP_207868.1; NC_000915.1.
DR RefSeq; WP_000780430.1; NC_018939.1.
DR AlphaFoldDB; Q48262; -.
DR DIP; DIP-3647N; -.
DR IntAct; Q48262; 4.
DR MINT; Q48262; -.
DR STRING; 85962.C694_05565; -.
DR TCDB; 2.A.52.1.4; the ni(2+)-co(2+) transporter (nicot) family.
DR PaxDb; Q48262; -.
DR EnsemblBacteria; AAD08119; AAD08119; HP_1077.
DR KEGG; hpy:HP_1077; -.
DR PATRIC; fig|85962.47.peg.1156; -.
DR eggNOG; COG3376; Bacteria.
DR OMA; VSKSWHI; -.
DR PhylomeDB; Q48262; -.
DR PHI-base; PHI:6850; -.
DR Proteomes; UP000000429; Chromosome.
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; Membrane; Nickel; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..331
FT /note="High-affinity nickel-transport protein NixA"
FT /id="PRO_0000194007"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:10692379"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 27..33
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:10692379"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 55..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:10692379"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 88..113
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:10692379"
FT TRANSMEM 114..135
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 136..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:10692379"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 200..225
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:10692379"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 247..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:10692379"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 274..302
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:10692379"
FT TRANSMEM 303..322
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 323..331
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:10692379"
FT CONFLICT 293..294
FT /note="RA -> NT (in Ref. 1; CAA88633)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="L -> F (in Ref. 1; CAA88633)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 331 AA; 37034 MW; C4EE36DDAAAD08EA CRC64;
MKLWFPYFLA IVFLHALGLA LLFMANNASF YAAASMAYML GAKHAFDADH IACIDNTIRK
LTQQGKNAYG VGFYFSMGHS SVVILMTIIS AFAIAWAKEH TPMLEEIGGV VGTLVSGLFL
LIIGLLNAII LLDLLKIFKK SHSNESLSQQ QNEEIERLLT SRGLLNRFFK PLFNFVSKSW
HIYPIGFLFG LGFDTASEIA LLALSSSAIK VSMVGMLSLP ILFAAGMSLF DTLDGAFMLK
AYDWAFKTPL RKIYYNISIT ALSVFIALFI GLIELFQVVS EKLHLKFENR LLRALQSLEF
TDLGYYLVGL FVIAFLGSFF LWKIKFSKLE S
