CNTB_STAAM
ID CNTB_STAAM Reviewed; 311 AA.
AC A0A0H3K104;
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 CntB {ECO:0000305};
GN Name=cntB {ECO:0000303|PubMed:27230378};
GN OrderedLocusNames=SAV2466 {ECO:0000312|EMBL:BAB58628.1};
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; BAB58628.1; -; Genomic_DNA.
DR RefSeq; WP_000472243.1; NC_002758.2.
DR AlphaFoldDB; A0A0H3K104; -.
DR SMR; A0A0H3K104; -.
DR PaxDb; A0A0H3K104; -.
DR EnsemblBacteria; BAB58628; BAB58628; SAV2466.
DR KEGG; sav:SAV2466; -.
DR HOGENOM; CLU_036879_0_2_9; -.
DR OMA; QLPWFTL; -.
DR PhylomeDB; A0A0H3K104; -.
DR BioCyc; SAUR158878:SAV_RS13460-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; IPR045621; BPD_transp_1_N.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 1.
DR Pfam; PF19300; BPD_transp_1_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..311
FT /note="Metal-staphylopine import system permease protein
FT CntB"
FT /id="PRO_0000447272"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 99..295
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 311 AA; 34749 MW; 6430180FC76CB38E CRC64;
MFKFILKRIA LMFPLVIVVS FMTFLLTYIT NENPAVTILH AQGTPNVTPE LIAETNEKYG
FNDPLLIQYK NWLLEAMQFN FGTSYITGDP VAERIGPAFM NTLKLTIISS VMVMITSIIL
GVVSALKRGK FTDRAIRSVA FFLTALPSYW IASILIIYVS VKLNILPTSG LTGPESYILP
VIVITIAYAG IYFRNVRRSM VEQLNEDYVL YLRASGVKSI TLMLHVLRNA IQVAVSIFCM
SIPMIMGGLV VIEYIFAWPG LGQLSLKAIL EHDFPVIQAY VLIVAVLFIV FNTLADIINA
LLNPRLREGA R
