ID   NIKD_STAAB              Reviewed;         257 AA.
AC   Q2YXY9;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Nickel import system ATP-binding protein NikD {ECO:0000250|UniProtKB:Q2FYQ7};
DE            EC=7.2.2.11 {ECO:0000250|UniProtKB:Q2FYQ7};
GN   Name=nikD {ECO:0000250|UniProtKB:Q2FYQ7}; Synonyms=oppD2;
GN   OrderedLocusNames=SAB1235c;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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:Q2FYQ7}.
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:Q2FYQ7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15558;
CC         Evidence={ECO:0000250|UniProtKB:Q2FYQ7};
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:Q2FYQ7}.
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; AJ938182; CAI80924.1; -; Genomic_DNA.
DR   RefSeq; WP_000052324.1; NC_007622.1.
DR   AlphaFoldDB; Q2YXY9; -.
DR   SMR; Q2YXY9; -.
DR   KEGG; sab:SAB1235c; -.
DR   HOGENOM; CLU_000604_1_23_9; -.
DR   OMA; THSFNDH; -.
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..257
FT                   /note="Nickel import system ATP-binding protein NikD"
FT                   /id="PRO_0000276792"
FT   DOMAIN          4..245
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         37..44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   257 AA;  29551 MW;  0EA4C8DCAFBB1032 CRC64;
     MSLIDIQNLT IKNTSEKSLI KGIDLKIFSQ QINALIGESG AGKSLIAKAL LEYLPFDLTC
     TYYSYQFDGE NVSRLSKYYG HTIGYISQNY AESFNDHTKL GKQLTAIYRK HYKSSKEEAL
     SKIDKALSWV NLQSKDILNK YSFQLSGGQL ERVYIASVLM LEPKLIIADE PVASLDALNG
     NQVMDLLQHI VLEHGQTLFI ITHNLSHVLK YCQYINVLKE GQIIEQGNID HFKYEHLHPY
     TEQLIKYRTQ LKRDYYD