NIKE_STAAW
ID NIKE_STAAW Reviewed; 233 AA.
AC Q8NWT6;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=MW1267;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
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; BA000033; BAB95132.1; -; Genomic_DNA.
DR RefSeq; WP_000571247.1; NC_003923.1.
DR AlphaFoldDB; Q8NWT6; -.
DR EnsemblBacteria; BAB95132; BAB95132; BAB95132.
DR KEGG; sam:MW1267; -.
DR HOGENOM; CLU_000604_1_23_9; -.
DR OMA; CDRTVHW; -.
DR Proteomes; UP000000418; 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_0000276806"
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
