NIKE_STAAS
ID NIKE_STAAS Reviewed; 233 AA.
AC Q6G9I1;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=SAS1320;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571857; CAG43096.1; -; Genomic_DNA.
DR RefSeq; WP_000571247.1; NC_002953.3.
DR AlphaFoldDB; Q6G9I1; -.
DR KEGG; sas:SAS1320; -.
DR HOGENOM; CLU_000604_1_23_9; -.
DR OMA; CDRTVHW; -.
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_0000276804"
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; 26229 MW; A3A48D7F0B3667B1 CRC64;
MIELKHVTFG YNKKQMVLQD INITIPDGEN VGILGESGCG KSTLASLVLG LFKPAKGEIY
LSDNAVLPIF QHPLTSFNPD WTIETSLKEA LYYYRGLTDN TAQDQLLLQH LSTFELNAQL
LTKLPSEVSG GQLQRFNVMR SLLAQPRVLI CDEITSNLDV IAEQNVINIL KAQTITNLNH
FIVISHDLSV LQRLVNRIIV LKDGMIVDDF AIEELFNVDR HPYTKELVQA FSY