NIKE_STAAN
ID NIKE_STAAN Reviewed; 233 AA.
AC Q7A5Q9;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=SA1211;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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; BA000018; BAB42471.1; -; Genomic_DNA.
DR PIR; C89914; C89914.
DR RefSeq; WP_000571259.1; NC_002745.2.
DR AlphaFoldDB; Q7A5Q9; -.
DR SMR; Q7A5Q9; -.
DR EnsemblBacteria; BAB42471; BAB42471; BAB42471.
DR KEGG; sau:SA1211; -.
DR HOGENOM; CLU_000604_1_23_9; -.
DR OMA; CDRTVHW; -.
DR Proteomes; UP000000751; 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_0000276807"
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; 26291 MW; E367D75B86C92B0B CRC64;
MIELKHVTFG YNKKQMVLQD INITIPDGEN VGILGESGCG KSTLASLVLG LFKPVKGEIY
LSDNAVLTIF QHPLTSFNPD WTIETSLKEA LYYYRGLTDN TAQDQLLLQH LSTFELNAQL
LTKLPSEVSG GQLQRFNVMR SLLAQPRVLI CDEITSNLDV IAEQNVINIL KAQTITNLNH
FIVISHDLSV LQRLVNRIIV LKDGMIVDDF AIEELFNVDR HPYTKELVQT FSY