CNTF_STAA8
ID CNTF_STAA8 Reviewed; 249 AA.
AC Q2FVF1; Q9ZGN8;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Metal-staphylopine import system ATP-binding protein CntF {ECO:0000305};
DE EC=7.2.2.- {ECO:0000305|PubMed:23279021};
GN Name=cntF {ECO:0000303|PubMed:23279021};
GN Synonyms=opp-1F {ECO:0000303|PubMed:9791183},
GN opp1F {ECO:0000303|PubMed:23279021};
GN OrderedLocusNames=SAOUHSC_02763 {ECO:0000312|EMBL:ABD31767.1};
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 [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=NCTC 8325 / PS 47;
RX PubMed=9791183; DOI=10.1046/j.1365-2958.1998.01075.x;
RA Coulter S.N., Schwan W.R., Ng E.Y.W., Langhorne M.H., Ritchie H.D.,
RA Westbrock-Wadman S., Hufnagle W.O., Folger K.R., Bayer A.S., Stover C.K.;
RT "Staphylococcus aureus genetic loci impacting growth and survival in
RT multiple infection environments.";
RL Mol. Microbiol. 30:393-404(1998).
RN [2]
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 [3]
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 [4]
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 (PubMed:23279021). Insertion mutant shows attenuated growth in several
CC infection models (PubMed:9791183). {ECO:0000269|PubMed:23279021,
CC ECO:0000269|PubMed:9791183}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC69841.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF076683; AAC69841.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP000253; ABD31767.1; -; Genomic_DNA.
DR RefSeq; WP_000590517.1; NZ_LS483365.1.
DR RefSeq; YP_501222.1; NC_007795.1.
DR AlphaFoldDB; Q2FVF1; -.
DR SMR; Q2FVF1; -.
DR STRING; 1280.SAXN108_2717; -.
DR TCDB; 3.A.1.5.43; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; ABD31767; ABD31767; SAOUHSC_02763.
DR GeneID; 3921635; -.
DR KEGG; sao:SAOUHSC_02763; -.
DR PATRIC; fig|93061.5.peg.2498; -.
DR eggNOG; COG1124; Bacteria.
DR HOGENOM; CLU_000604_1_23_9; -.
DR OMA; NPLFTIQ; -.
DR Proteomes; UP000008816; 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: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; Ion transport;
KW Membrane; Nickel; Nickel transport; Nucleotide-binding; Reference proteome;
KW Translocase; Transport; Zinc; Zinc transport.
FT CHAIN 1..249
FT /note="Metal-staphylopine import system ATP-binding protein
FT CntF"
FT /id="PRO_0000447277"
FT DOMAIN 2..244
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 117
FT /note="E -> D (in Ref. 1; AAC69841)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 249 AA; 28180 MW; 59C6007D31C917CE CRC64;
MIKIKDVEKS YQSAHVFKRR RTPIVKGVSF ECPIGATIAI IGESGSGKST LSRMILGIEK
PDKGCVTLND QPMHKKKVRR HQIGAVFQDY TSSLHPFQTV REILFEVMCQ CDGQPKEVME
VQAITLLEEV GLSKAYMDKY PNMLSGGEAQ RVAIARAICI NPKYILFDEA ISSLDMSIQT
QILDLLIHLR ETRQLSYIFI THDIQAATYL CDQLIIFKNG KIEEQIPTSA LHKSDNAYTR
ELIEKQLSF
