ID   CNTD_STAA8              Reviewed;         271 AA.
AC   Q2FVF0;
DT   05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Metal-staphylopine import system ATP-binding protein CntD {ECO:0000305};
DE            EC=7.2.2.- {ECO:0000305|PubMed:23279021};
GN   Name=cntD {ECO:0000303|PubMed:23279021};
GN   Synonyms=opp1D {ECO:0000303|PubMed:23279021};
GN   OrderedLocusNames=SAOUHSC_02764 {ECO:0000312|EMBL:ABD31768.1};
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 [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   [2]
RP   FUNCTION, ACTIVITY REGULATION, SUBUNIT, INDUCTION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=RN6390;
RX   PubMed=23279021; DOI=10.1111/mmi.12126;
RA   Remy L., Carriere M., Derre-Bobillot A., Martini C., Sanguinetti M.,
RA   Borezee-Durant E.;
RT   "The Staphylococcus aureus Opp1 ABC transporter imports nickel and cobalt
RT   in zinc-depleted conditions and contributes to virulence.";
RL   Mol. Microbiol. 87:730-743(2013).
RN   [3]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=29581261; DOI=10.1073/pnas.1718382115;
RA   Song L., Zhang Y., Chen W., Gu T., Zhang S.Y., Ji Q.;
RT   "Mechanistic insights into staphylopine-mediated metal acquisition.";
RL   Proc. Natl. Acad. Sci. U.S.A. 115:3942-3947(2018).
CC   -!- FUNCTION: Part of the ABC transporter complex CntABCDF (Opp1) involved
CC       in the uptake of metal in complex with the metallophore staphylopine
CC       (StP). Involved in the import of divalent metals ions such as nickel,
CC       cobalt and zinc. Probably responsible for energy coupling to the
CC       transport system (PubMed:23279021, PubMed:29581261). Plays a major role
CC       in nickel/cobalt import in zinc-depleted conditions. Contributes to
CC       virulence. Required for full urease activity in vitro
CC       (PubMed:23279021). {ECO:0000269|PubMed:23279021,
CC       ECO:0000269|PubMed:29581261}.
CC   -!- ACTIVITY REGULATION: Nickel/cobalt import is reduced in the presence of
CC       zinc. {ECO:0000269|PubMed:23279021}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (CntD and
CC       CntF), two transmembrane proteins (CntB and CntC) and a solute-binding
CC       protein (CntA). {ECO:0000305|PubMed:23279021,
CC       ECO:0000305|PubMed:29581261}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: Repressed by zinc. {ECO:0000269|PubMed:23279021}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the cntABCDF genes decreases nickel
CC       and cobalt intracellular levels and decreases virulence.
CC       {ECO:0000269|PubMed:23279021}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; CP000253; ABD31768.1; -; Genomic_DNA.
DR   RefSeq; WP_000173869.1; NZ_LS483365.1.
DR   RefSeq; YP_501223.1; NC_007795.1.
DR   AlphaFoldDB; Q2FVF0; -.
DR   SMR; Q2FVF0; -.
DR   STRING; 1280.SAXN108_2718; -.
DR   TCDB; 3.A.1.5.43; the atp-binding cassette (abc) superfamily.
DR   EnsemblBacteria; ABD31768; ABD31768; SAOUHSC_02764.
DR   GeneID; 3921419; -.
DR   KEGG; sao:SAOUHSC_02764; -.
DR   PATRIC; fig|93061.5.peg.2499; -.
DR   eggNOG; COG0444; Bacteria.
DR   HOGENOM; CLU_000604_1_23_9; -.
DR   OMA; PHGRVKA; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0006824; P:cobalt ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0015675; P:nickel cation transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006829; P:zinc ion transport; 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; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Cobalt; Cobalt transport; Ion transport;
KW   Membrane; Nickel; Nickel transport; Nucleotide-binding; Reference proteome;
KW   Translocase; Transport; Zinc; Zinc transport.
FT   CHAIN           1..271
FT                   /note="Metal-staphylopine import system ATP-binding protein
FT                   CntD"
FT                   /id="PRO_0000447275"
FT   DOMAIN          6..251
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         38..45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   271 AA;  30469 MW;  FB442E1B89FC0547 CRC64;
     MTLLTVKHLT ITDTWTDQPL VSDVNFTLTK GETLGVIGES GSGKSITCKS IIGLNPERLG
     VTGEIIFDGT SMLSLSESQL KKYRGKDIAM VMQQGSRAFD PSTTVGKQMF ETMKVHTSMS
     TQEIEKTLIE YMDYLSLKDP KRILKSYPYM LSGGMLQRLM IALALALKPK LIIADEPTTA
     LDTITQYDVL EAFIDIKKHF DCAMIFISHD LTVINKIADR VVVMKNGQLI EQGTRESVLH
     HPEHVYTKYL LSTKKKINDH FKHVMRGDVH D