CNTA_STAAM
ID CNTA_STAAM Reviewed; 532 AA.
AC A0A0H3JTL0;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Metal-staphylopine-binding protein CntA {ECO:0000305};
DE Flags: Precursor;
GN Name=cntA {ECO:0000303|PubMed:27230378};
GN OrderedLocusNames=SAV2467 {ECO:0000312|EMBL:BAB58629.1};
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. Binds the
CC metal via the metallophore StP, and transfers the StP-metal complex to
CC the membrane-bound permease. {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:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
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 bacterial solute-binding protein 5 family.
CC {ECO:0000305}.
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DR EMBL; BA000017; BAB58629.1; -; Genomic_DNA.
DR RefSeq; WP_001229087.1; NC_002758.2.
DR AlphaFoldDB; A0A0H3JTL0; -.
DR SMR; A0A0H3JTL0; -.
DR PaxDb; A0A0H3JTL0; -.
DR EnsemblBacteria; BAB58629; BAB58629; SAV2467.
DR KEGG; sav:SAV2467; -.
DR HOGENOM; CLU_017028_7_5_9; -.
DR OMA; GEHEMAF; -.
DR PhylomeDB; A0A0H3JTL0; -.
DR BioCyc; SAUR158878:SAV_RS13465-MON; -.
DR Proteomes; UP000002481; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProt.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
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; cd08489; PBP2_NikA; 1.
DR InterPro; IPR011980; NikA_ABC_Ni-bd.
DR InterPro; IPR030678; Peptide/Ni-bd.
DR InterPro; IPR039424; SBP_5.
DR InterPro; IPR023765; SBP_5_CS.
DR InterPro; IPR000914; SBP_5_dom.
DR PANTHER; PTHR30290; PTHR30290; 1.
DR Pfam; PF00496; SBP_bac_5; 1.
DR PIRSF; PIRSF002741; MppA; 1.
DR TIGRFAMs; TIGR02294; nickel_nikA; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS01040; SBP_BACTERIAL_5; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cobalt; Cobalt transport; Copper; Copper transport;
KW Ion transport; Iron; Iron transport; Lipoprotein; Membrane; Nickel;
KW Nickel transport; Palmitate; Signal; Transport; Zinc; Zinc transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 21..532
FT /note="Metal-staphylopine-binding protein CntA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT /id="PRO_5002612961"
FT BINDING 165
FT /ligand="staphylopine"
FT /ligand_id="ChEBI:CHEBI:141669"
FT /evidence="ECO:0000250|UniProtKB:Q2FVE7"
FT BINDING 418
FT /ligand="staphylopine"
FT /ligand_id="ChEBI:CHEBI:141669"
FT /evidence="ECO:0000250|UniProtKB:Q2FVE7"
FT BINDING 448
FT /ligand="staphylopine"
FT /ligand_id="ChEBI:CHEBI:141669"
FT /evidence="ECO:0000250|UniProtKB:Q2FVE7"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 532 AA; 60022 MW; B2F2B506B7BEBD2E CRC64;
MRKLTKMSAM LLASGLILTG CGGNKGLEEK KENKQLTYTT VKDIGDMNPH VYGGSMSAES
MIYEPLVRNT KDGIKPLLAK KWDVSEDGKT YTFHLRDDVK FHDGTTFDAD AVKKNIDAVQ
QNKKLHSWLK ISTLIDNVKV KDKYTVELNL KEAYQPALAE LAMPRPYVFV SPKDFKNGTT
KDGVKKFDGT GPFKLGEHKK DESADFNKND QYWGEKSKLN KVQAKVMPAG ETAFLSMKKG
ETNFAFTDDR GTDSLDKDSL KQLKDTGDYQ VKRSQPMNTK MLVVNSGKKD NAVSDKTVRQ
AIGHMVNRDK IAKEILDGQE KPATQLFAKN VTDINFDMPT RKYDLKKAES LLDEAGWKKG
KDSDVRQKDG KNLEMAMYYD KGSSSQKEQA EYLQAEFKKM GIKLNINGET SDKIAERRTS
GDYDLMFNQT WGLLYDPQST IAAFKAKNGY ESATSGIENK DKIYNSIDDA FKIQNGKERS
DAYKNILKQI DDEGIFIPIS HGSMTVVAPK DLEKVSFTQS QYELPFNEMQ YK
