CNTF_STAAM
ID CNTF_STAAM Reviewed; 249 AA.
AC A0A0H3JT74;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Metal-staphylopine import system ATP-binding protein CntF {ECO:0000305};
DE EC=7.2.2.- {ECO:0000305|PubMed:27230378};
GN Name=cntF {ECO:0000303|PubMed:27230378};
GN OrderedLocusNames=SAV2463 {ECO:0000312|EMBL:BAB58625.1};
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}.
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; BA000017; BAB58625.1; -; Genomic_DNA.
DR RefSeq; WP_000598772.1; NC_002758.2.
DR AlphaFoldDB; A0A0H3JT74; -.
DR SMR; A0A0H3JT74; -.
DR PaxDb; A0A0H3JT74; -.
DR EnsemblBacteria; BAB58625; BAB58625; SAV2463.
DR KEGG; sav:SAV2463; -.
DR HOGENOM; CLU_000604_1_23_9; -.
DR OMA; NPLFTIQ; -.
DR PhylomeDB; A0A0H3JT74; -.
DR BioCyc; SAUR158878:SAV_RS13445-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..249
FT /note="Metal-staphylopine import system ATP-binding protein
FT CntF"
FT /id="PRO_0000447278"
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"
SQ SEQUENCE 249 AA; 28124 MW; C44699FBE6A21C01 CRC64;
MIKVTDVEKS YQSAHVFKRR RTPIVKGVSF ECPIGATIAI IGESGSGKST LSRMILGIEK
PDKGCVTLND LPMHKKKVRR HQIGAVFQDY TSSLHPFQTV REILFEVMCQ CDGQPKEVME
VQAITLLEEV GLSKAYMDKY PNMLSGGEAQ RVAIARAICI NPKYILFDEA ISSLDMSIQT
QILDLLIHLR ETRQLSYIFI THDIQAATYL CDQLIIFKNG KIEEQIPTSA LHKSDNAYTR
ELIEKQLSF
