ID CNTC_STAA8 Reviewed; 289 AA. AC Q2FVE9; DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 03-JUL-2019, entry version 92. DE RecName: Full=Metal-staphylopine import system permease protein CntC {ECO:0000305}; GN Name=cntC {ECO:0000303|PubMed:23279021}; GN Synonyms=opp1C {ECO:0000303|PubMed:23279021}; GN OrderedLocusNames=SAOUHSC_02765 {ECO:0000312|EMBL:ABD31769.1}; OS Staphylococcus aureus (strain NCTC 8325). 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; RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., RA 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, RL Washington 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 RT cobalt 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) CC involved in the uptake of metal in complex with the metallophore CC staphylopine (StP). Involved in the import of divalent metals ions CC such as nickel, cobalt and zinc. Probably responsible for the CC translocation of the substrate across the membrane CC (PubMed:23279021, PubMed:29581261). Plays a major role in CC 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 CC presence of zinc. {ECO:0000269|PubMed:23279021}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (CntD CC and CntF), two transmembrane proteins (CntB and CntC) and a CC solute-binding protein (CntA). {ECO:0000305|PubMed:23279021, CC ECO:0000305|PubMed:29581261}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000255}. CC -!- INDUCTION: Repressed by zinc. {ECO:0000269|PubMed:23279021}. CC -!- DISRUPTION PHENOTYPE: Deletion of the cntABCDF genes decreases CC nickel and cobalt intracellular levels and decreases virulence. CC {ECO:0000269|PubMed:23279021}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000253; ABD31769.1; -; Genomic_DNA. DR RefSeq; WP_000584765.1; NZ_LS483365.1. DR RefSeq; YP_501224.1; NC_007795.1. DR STRING; 1280.SAXN108_2719; -. DR TCDB; 3.A.1.5.43; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; ABD31769; ABD31769; SAOUHSC_02765. DR GeneID; 3921420; -. DR KEGG; sao:SAOUHSC_02765; -. DR PATRIC; fig|93061.5.peg.2500; -. DR eggNOG; ENOG4105C2T; Bacteria. DR eggNOG; COG1173; LUCA. DR HOGENOM; HOG000171368; -. DR KO; K15586; -. DR OMA; FSMRIGT; -. DR BioCyc; GCF_000013425:G1I0R-2605-MONOMER; -. DR BioCyc; SAUR93061:G1G5Y-2605-MONOMER; -. DR Proteomes; UP000008816; 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:0015675; P:nickel cation transport; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. 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; Complete proteome; KW Ion transport; Membrane; Nickel; Nickel transport; Reference proteome; KW Transmembrane; Transmembrane helix; Transport; Zinc; Zinc transport. FT CHAIN 1 289 Metal-staphylopine import system permease FT protein CntC. FT /FTId=PRO_0000447273. FT TRANSMEM 13 33 Helical. {ECO:0000255}. FT TRANSMEM 77 97 Helical. {ECO:0000255}. FT TRANSMEM 115 135 Helical. {ECO:0000255}. FT TRANSMEM 194 214 Helical. {ECO:0000255}. FT TRANSMEM 249 269 Helical. {ECO:0000255}. FT DOMAIN 73 262 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 289 AA; 31965 MW; 8CA7ED6E4E4CC8F6 CRC64; MIILKRLLQD KGAVIALGII VLYVFLGLAA PLVTFYDPNH IDTANKFAGM SFQHLLGTDH LGRDILTRLI YAIRPSLLYV FVALFVSVLI GSILGFLSGY FQGFVDALIM RACDVMLAFP SYVVTLALIA LFGMGAENII MAFILTRWAW FCRVIRTSVM QYTASDHVRF AKTIGMNDMK IIHKHIMPLT LADIAIISSS SMCSMILQIS GFSFLGLGVK APTAEWGMML NEARKVMFTH PEMMFAPGIA IVIIVMAFNF LSDALQIAID PRISSKDKLR SVKKGVVQS //