CNTC_STAA8
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 25-MAY-2022, entry version 103.
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 / 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 the translocation of the
CC substrate across the membrane (PubMed:23279021, PubMed:29581261). Plays
CC a major role in nickel/cobalt import in zinc-depleted conditions.
CC Contributes to 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}; Multi-pass membrane
CC protein {ECO:0000255}.
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 binding-protein-dependent transport system
CC permease family. {ECO:0000305}.
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DR EMBL; CP000253; ABD31769.1; -; Genomic_DNA.
DR RefSeq; WP_000584765.1; NZ_LS483365.1.
DR RefSeq; YP_501224.1; NC_007795.1.
DR AlphaFoldDB; Q2FVE9; -.
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; COG1173; Bacteria.
DR HOGENOM; CLU_028518_1_1_9; -.
DR OMA; WFAVLPN; -.
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: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; Ion transport; Membrane; Nickel;
KW Nickel transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport; Zinc; Zinc transport.
FT CHAIN 1..289
FT /note="Metal-staphylopine import system permease protein
FT CntC"
FT /id="PRO_0000447273"
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; 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
