ID   CNTC_STAAM              Reviewed;         289 AA.
AC   A0A0H3JU73;
DT   05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Metal-staphylopine import system permease protein CntC {ECO:0000305};
GN   Name=cntC {ECO:0000303|PubMed:27230378};
GN   OrderedLocusNames=SAV2465 {ECO:0000312|EMBL:BAB58627.1};
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 the translocation of the substrate across the membrane.
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}; Multi-pass membrane
CC       protein {ECO:0000255}.
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 binding-protein-dependent transport system
CC       permease family. {ECO:0000305}.
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DR   EMBL; BA000017; BAB58627.1; -; Genomic_DNA.
DR   RefSeq; WP_000584759.1; NC_002758.2.
DR   AlphaFoldDB; A0A0H3JU73; -.
DR   PaxDb; A0A0H3JU73; -.
DR   EnsemblBacteria; BAB58627; BAB58627; SAV2465.
DR   KEGG; sav:SAV2465; -.
DR   HOGENOM; CLU_028518_1_1_9; -.
DR   OMA; WFAVLPN; -.
DR   PhylomeDB; A0A0H3JU73; -.
DR   BioCyc; SAUR158878:SAV_RS13455-MON; -.
DR   Proteomes; UP000002481; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   CDD; cd06261; TM_PBP2; 1.
DR   Gene3D; 1.10.3720.10; -; 1.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   InterPro; IPR025966; OppC_N.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   Pfam; PF12911; OppC_N; 1.
DR   SUPFAM; SSF161098; SSF161098; 1.
DR   PROSITE; PS50928; ABC_TM1; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cobalt; Cobalt transport; Copper; Copper transport;
KW   Ion transport; Iron; Iron transport; Membrane; Nickel; Nickel transport;
KW   Transmembrane; Transmembrane helix; Transport; Zinc; Zinc transport.
FT   CHAIN           1..289
FT                   /note="Metal-staphylopine import system permease protein
FT                   CntC"
FT                   /id="PRO_0000447274"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        249..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          73..262
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   289 AA;  31947 MW;  10D62A7123FA139A CRC64;
     MIILKRLLQD KGAVIALGII VLYVFLGLAA PLVTFYDPNH IDTANKFAGI SFQHLLGTDH
     LGRDILTRLI YAIRPSLLYV FVALFVSVLI GSILGFLSGY FQGFVDALIM RACDVMLAFP
     SYVVTLALIA LFGMGAENII MAFILTRWAW FCRVIRTSVM QYTASDHVRF AKTIGMNDMK
     IIHKHIMPLT LADIAIISSS SMCSMILQIS GFSFLGLGVK APTAEWGMML NEARKVMFTH
     PEMMFAPGIA IVIIVMAFNF LSDALQIAID PRISSKDKLR SVKKGVVQS