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NIKE_STAA3
ID   NIKE_STAA3              Reviewed;         233 AA.
AC   Q2FH58;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Nickel import system ATP-binding protein NikE {ECO:0000250|UniProtKB:Q2FYQ8};
DE            EC=7.2.2.11 {ECO:0000250|UniProtKB:Q2FYQ8};
GN   Name=nikE {ECO:0000250|UniProtKB:Q2FYQ8}; Synonyms=oppF2;
GN   OrderedLocusNames=SAUSA300_1273;
OS   Staphylococcus aureus (strain USA300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=367830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300;
RX   PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA   Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA   Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA   Perdreau-Remington F.;
RT   "Complete genome sequence of USA300, an epidemic clone of community-
RT   acquired meticillin-resistant Staphylococcus aureus.";
RL   Lancet 367:731-739(2006).
CC   -!- FUNCTION: Part of the ABC transporter complex NikABCDE (Opp2) involved
CC       in nickel import. Probably responsible for energy coupling to the
CC       transport system. {ECO:0000250|UniProtKB:Q2FYQ8}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + Ni(2+)(out) = ADP + H(+) + Ni(2+)(in) + phosphate;
CC         Xref=Rhea:RHEA:15557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49786,
CC         ChEBI:CHEBI:456216; EC=7.2.2.11;
CC         Evidence={ECO:0000250|UniProtKB:Q2FYQ8};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15558;
CC         Evidence={ECO:0000250|UniProtKB:Q2FYQ8};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (NikD and
CC       NikE), two transmembrane proteins (NikB and NikC) and a solute-binding
CC       protein (NikA). {ECO:0000250|UniProtKB:Q2FYQ8}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; CP000255; ABD21447.1; -; Genomic_DNA.
DR   RefSeq; WP_000571258.1; NZ_CP027476.1.
DR   AlphaFoldDB; Q2FH58; -.
DR   SMR; Q2FH58; -.
DR   EnsemblBacteria; ABD21447; ABD21447; SAUSA300_1273.
DR   KEGG; saa:SAUSA300_1273; -.
DR   HOGENOM; CLU_000604_1_23_9; -.
DR   OMA; CDRTVHW; -.
DR   Proteomes; UP000001939; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015413; F:ABC-type nickel transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Ion transport; Membrane; Nickel;
KW   Nickel transport; Nucleotide-binding; Translocase; Transport.
FT   CHAIN           1..233
FT                   /note="Nickel import system ATP-binding protein NikE"
FT                   /id="PRO_0000276808"
FT   DOMAIN          2..228
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         35..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   233 AA;  26257 MW;  C3B38342B3DE9673 CRC64;
     MIELKHVTFG YNKKQMVLQD INITIPDGEN VGILGESGCG KSTLASLVLG LFKPVKGEIY
     LSDNAVLPIF QHPLTSFNPD WTIETSLKEA LYYYRGLTDN TAQDQLLLQH LSTFELNAQL
     LTKLPSEVSG GQLQRFNVMR SLLAQPRVLI CDEITSNLDV IAEQNVINIL KAQTITNLNH
     FIVISHDLSV LQRLVNRIIV LKDGMIVDDF AIEELFNVDR HPYTKELVQA FSY
 
 
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