NIKE_STAA8
ID NIKE_STAA8 Reviewed; 233 AA.
AC Q2FYQ8; Q84AN4; Q9ZGN3;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Nickel import system ATP-binding protein NikE {ECO:0000305};
DE EC=7.2.2.11 {ECO:0000305|PubMed:20662775};
GN Name=nikE {ECO:0000303|PubMed:20662775}; Synonyms=opp-2F, oppF2;
GN OrderedLocusNames=SAOUHSC_01377;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RX PubMed=9791183; DOI=10.1046/j.1365-2958.1998.01075.x;
RA Coulter S.N., Schwan W.R., Ng E.Y.W., Langhorne M.H., Ritchie H.D.,
RA Westbrock-Wadman S., Hufnagle W.O., Folger K.R., Bayer A.S., Stover C.K.;
RT "Staphylococcus aureus genetic loci impacting growth and survival in
RT multiple infection environments.";
RL Mol. Microbiol. 30:393-404(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Cramton S.E., Madimidou F., Goetz F.;
RT "Role of the oligopeptide permease (opp-2) operon in Staphylococcus aureus
RT biofilm formation.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=RN6390;
RX PubMed=20662775; DOI=10.1111/j.1365-2958.2010.07287.x;
RA Hiron A., Posteraro B., Carriere M., Remy L., Delporte C., La Sorda M.,
RA Sanguinetti M., Juillard V., Borezee-Durant E.;
RT "A nickel ABC-transporter of Staphylococcus aureus is involved in urinary
RT tract infection.";
RL Mol. Microbiol. 77:1246-1260(2010).
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. Required for full urease activity and plays a
CC significant role in the virulence of S.aureus during urinary tract
CC infection (UTI). {ECO:0000269|PubMed:20662775}.
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:0000305|PubMed:20662775};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15558;
CC Evidence={ECO:0000305|PubMed:20662775};
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:0000269|PubMed:20662775}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Transcription is stable during the exponential phase and
CC increases only in standard conditions in late exponential phase.
CC {ECO:0000269|PubMed:20662775}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the nikBCDE operon strongly reduces
CC nickel transport and urease activity. Mutant shows decreased virulence
CC in a mouse model of ascending UTI (PubMed:20662775). Insertion mutant
CC shows attenuated growth in several infection models (PubMed:9791183).
CC {ECO:0000269|PubMed:20662775, ECO:0000269|PubMed:9791183}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; AF076684; AAC69846.1; -; Genomic_DNA.
DR EMBL; AY205146; AAO47758.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD30472.1; -; Genomic_DNA.
DR RefSeq; WP_000571258.1; NZ_LS483365.1.
DR RefSeq; YP_499904.1; NC_007795.1.
DR AlphaFoldDB; Q2FYQ8; -.
DR SMR; Q2FYQ8; -.
DR STRING; 1280.SAXN108_1394; -.
DR EnsemblBacteria; ABD30472; ABD30472; SAOUHSC_01377.
DR GeneID; 3920786; -.
DR KEGG; sao:SAOUHSC_01377; -.
DR PATRIC; fig|93061.5.peg.1261; -.
DR eggNOG; COG4608; Bacteria.
DR HOGENOM; CLU_000604_1_23_9; -.
DR OMA; CDRTVHW; -.
DR PRO; PR:Q2FYQ8; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015413; F:ABC-type nickel transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Ion transport; Membrane; Nickel;
KW Nickel transport; Nucleotide-binding; Reference proteome; Translocase;
KW Transport.
FT CHAIN 1..233
FT /note="Nickel import system ATP-binding protein NikE"
FT /id="PRO_0000272188"
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"
FT CONFLICT 203
FT /note="D -> N (in Ref. 2; AAO47758)"
FT /evidence="ECO:0000305"
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
