ID   CNTD_STAAM              Reviewed;         271 AA.
AC   A0A0H3JXA3;
DT   05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Metal-staphylopine import system ATP-binding protein CntD {ECO:0000305};
DE            EC=7.2.2.- {ECO:0000305|PubMed:27230378};
GN   Name=cntD {ECO:0000303|PubMed:27230378};
GN   OrderedLocusNames=SAV2464 {ECO:0000312|EMBL:BAB58626.1};
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
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).
RN   [2]
RP   FUNCTION, SUBUNIT, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=27230378; DOI=10.1126/science.aaf1018;
RA   Ghssein G., Brutesco C., Ouerdane L., Fojcik C., Izaute A., Wang S.,
RA   Hajjar C., Lobinski R., Lemaire D., Richaud P., Voulhoux R., Espaillat A.,
RA   Cava F., Pignol D., Borezee-Durant E., Arnoux P.;
RT   "Biosynthesis of a broad-spectrum nicotianamine-like metallophore in
RT   Staphylococcus aureus.";
RL   Science 352:1105-1109(2016).
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). May be involved in the import of a large array of divalent
CC       metals ions such as nickel, cobalt, zinc, copper and iron. Probably
CC       responsible for energy coupling to the transport system.
CC       {ECO:0000269|PubMed:27230378}.
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:27230378}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: Up-regulated in metal-poor media.
CC       {ECO:0000269|PubMed:27230378}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the cntABCDF genes decreases StP
CC       intracellular levels and decreases the import of iron, zinc, nickel and
CC       cobalt. {ECO:0000269|PubMed:27230378}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; BA000017; BAB58626.1; -; Genomic_DNA.
DR   RefSeq; WP_000173871.1; NC_002758.2.
DR   AlphaFoldDB; A0A0H3JXA3; -.
DR   SMR; A0A0H3JXA3; -.
DR   PaxDb; A0A0H3JXA3; -.
DR   EnsemblBacteria; BAB58626; BAB58626; SAV2464.
DR   KEGG; sav:SAV2464; -.
DR   HOGENOM; CLU_000604_1_23_9; -.
DR   OMA; PHGRVKA; -.
DR   PhylomeDB; A0A0H3JXA3; -.
DR   BioCyc; SAUR158878:SAV_RS13450-MON; -.
DR   Proteomes; UP000002481; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006824; P:cobalt ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR   GO; GO:0015675; P:nickel cation transport; IEA:UniProtKB-KW.
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; Copper;
KW   Copper transport; Ion transport; Iron; Iron transport; Membrane; Nickel;
KW   Nickel transport; Nucleotide-binding; Translocase; Transport; Zinc;
KW   Zinc transport.
FT   CHAIN           1..271
FT                   /note="Metal-staphylopine import system ATP-binding protein
FT                   CntD"
FT                   /id="PRO_0000447276"
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;  30521 MW;  B1521CF75CDC167C CRC64;
     MTLLTVKHLT ITDTWTDQPL VSDVNFTLTK GETLGVIGES GSGKSITCKS IIGLNPERLG
     VTGEIIFDGT SMLSLSESQR KKYRGKDIAM VMQQGSRAFD PSTTVGKQMF ETMKVHTSMS
     TQEIEKTLIE YMDYLSLKDP KRILKSYPYM LSGGMLQRLM IALALALKPK LIIADEPTTA
     LDTITQYDVL EAFIDIKKHF DCAMIFISHD LTVINKIADR VVVMKNGQLI EHGTRESVLH
     HPEHVYTKYL LSTKKKINDH FKHVMRGDVH D