CNTA_STAA8
ID CNTA_STAA8 Reviewed; 532 AA.
AC Q2FVE7; Q9ZGP2;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Metal-staphylopine-binding protein CntA {ECO:0000305};
DE Flags: Precursor;
GN Name=cntA {ECO:0000303|PubMed:23279021};
GN Synonyms=opp-1A {ECO:0000303|PubMed:9791183},
GN opp1A {ECO:0000303|PubMed:23279021};
GN OrderedLocusNames=SAOUHSC_02767 {ECO:0000312|EMBL:ABD31771.1};
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-532, AND DISRUPTION PHENOTYPE.
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 [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] {ECO:0007744|PDB:5YH5, ECO:0007744|PDB:5YH8, ECO:0007744|PDB:5YHE, ECO:0007744|PDB:5YHG}
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 26-532 OF APOPROTEIN AND IN
RP COMPLEXES WITH STAPHYLOPINE; NICKEL; COBALT AND ZINC, FUNCTION, SUBUNIT,
RP DOMAIN, AND MUTAGENESIS OF TYR-52; TRP-128; ARG-165; ARG-250; ARG-418;
RP TRP-431; TYR-435; ASN-448 AND TYR-522.
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. Binds the metal via the metallophore StP, and
CC transfers the StP-metal complex to the membrane-bound permease
CC (PubMed:23279021, PubMed:29581261). Binds one molecule of StP/metal.
CC Binds StP/Co(2+) and StP/Ni(2+) tighter than StP/Zn(2+)
CC (PubMed:29581261). Plays a major role in nickel/cobalt import in zinc-
CC depleted conditions. Contributes to virulence. Required for full urease
CC activity in vitro (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:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- INDUCTION: Repressed by zinc. {ECO:0000269|PubMed:23279021}.
CC -!- DOMAIN: StP/metal binding triggers a notable interdomain conformational
CC change. {ECO:0000269|PubMed:29581261}.
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 bacterial solute-binding protein 5 family.
CC {ECO:0000305}.
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DR EMBL; CP000253; ABD31771.1; -; Genomic_DNA.
DR EMBL; AF076683; AAC69837.1; -; Genomic_DNA.
DR RefSeq; WP_001229079.1; NZ_LS483365.1.
DR RefSeq; YP_501226.1; NC_007795.1.
DR PDB; 5YH5; X-ray; 2.90 A; A=26-532.
DR PDB; 5YH8; X-ray; 2.12 A; A=26-532.
DR PDB; 5YHE; X-ray; 2.46 A; A/B=26-532.
DR PDB; 5YHG; X-ray; 2.03 A; A=26-532.
DR PDBsum; 5YH5; -.
DR PDBsum; 5YH8; -.
DR PDBsum; 5YHE; -.
DR PDBsum; 5YHG; -.
DR AlphaFoldDB; Q2FVE7; -.
DR SMR; Q2FVE7; -.
DR STRING; 1280.SAXN108_2721; -.
DR TCDB; 3.A.1.5.43; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; ABD31771; ABD31771; SAOUHSC_02767.
DR GeneID; 3921422; -.
DR KEGG; sao:SAOUHSC_02767; -.
DR PATRIC; fig|93061.5.peg.2502; -.
DR eggNOG; COG0747; Bacteria.
DR HOGENOM; CLU_017028_7_5_9; -.
DR OMA; GEHEMAF; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR GO; GO:1904680; F:peptide transmembrane transporter activity; IBA:GO_Central.
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:0015833; P:peptide transport; IBA:GO_Central.
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 3D-structure; Cell membrane; Cobalt; Cobalt transport; Ion transport;
KW Lipoprotein; Membrane; Nickel; Nickel transport; Palmitate;
KW Reference proteome; 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_5004208116"
FT BINDING 165
FT /ligand="staphylopine"
FT /ligand_id="ChEBI:CHEBI:141669"
FT /evidence="ECO:0000269|PubMed:29581261,
FT ECO:0007744|PDB:5YH8, ECO:0007744|PDB:5YHE,
FT ECO:0007744|PDB:5YHG"
FT BINDING 418
FT /ligand="staphylopine"
FT /ligand_id="ChEBI:CHEBI:141669"
FT /evidence="ECO:0000269|PubMed:29581261,
FT ECO:0007744|PDB:5YH8, ECO:0007744|PDB:5YHE,
FT ECO:0007744|PDB:5YHG"
FT BINDING 448
FT /ligand="staphylopine"
FT /ligand_id="ChEBI:CHEBI:141669"
FT /evidence="ECO:0000269|PubMed:29581261,
FT ECO:0007744|PDB:5YH8, ECO:0007744|PDB:5YHE,
FT ECO:0007744|PDB:5YHG"
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"
FT MUTAGEN 52
FT /note="Y->A: Strong decrease in StP/metal binding."
FT /evidence="ECO:0000269|PubMed:29581261"
FT MUTAGEN 128
FT /note="W->A: Strong decrease in StP/metal binding."
FT /evidence="ECO:0000269|PubMed:29581261"
FT MUTAGEN 165
FT /note="R->A: Does not bind StP/metal. Significantly reduces
FT metal accumulation."
FT /evidence="ECO:0000269|PubMed:29581261"
FT MUTAGEN 250
FT /note="R->A: Does not bind StP/metal."
FT /evidence="ECO:0000269|PubMed:29581261"
FT MUTAGEN 418
FT /note="R->A: Does not bind StP/metal."
FT /evidence="ECO:0000269|PubMed:29581261"
FT MUTAGEN 431
FT /note="W->A: Does not bind StP/metal. Significantly reduces
FT metal accumulation."
FT /evidence="ECO:0000269|PubMed:29581261"
FT MUTAGEN 435
FT /note="Y->A: Strong decrease in StP/metal binding. Slightly
FT reduces metal accumulation."
FT /evidence="ECO:0000269|PubMed:29581261"
FT MUTAGEN 448
FT /note="N->A: Slight decrease in StP/metal binding. Slightly
FT reduces metal accumulation."
FT /evidence="ECO:0000269|PubMed:29581261"
FT MUTAGEN 522
FT /note="Y->A: Does not bind StP/metal."
FT /evidence="ECO:0000269|PubMed:29581261"
FT CONFLICT 26..32
FT /note="GLEEKKE -> DSLGRKR (in Ref. 2; AAC69837)"
FT /evidence="ECO:0000305"
FT HELIX 27..32
FT /evidence="ECO:0007829|PDB:5YHG"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:5YHG"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:5YH5"
FT HELIX 56..62
FT /evidence="ECO:0007829|PDB:5YHG"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:5YHG"
FT STRAND 73..84
FT /evidence="ECO:0007829|PDB:5YHG"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:5YHE"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:5YHG"
FT HELIX 109..120
FT /evidence="ECO:0007829|PDB:5YHG"
FT HELIX 121..126
FT /evidence="ECO:0007829|PDB:5YHG"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:5YHG"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:5YHG"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:5YHG"
FT HELIX 157..161
FT /evidence="ECO:0007829|PDB:5YHG"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:5YHG"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:5YHG"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:5YHG"
FT STRAND 190..199
FT /evidence="ECO:0007829|PDB:5YHG"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:5YHG"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:5YHG"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:5YHG"
FT STRAND 218..226
FT /evidence="ECO:0007829|PDB:5YHG"
FT HELIX 231..238
FT /evidence="ECO:0007829|PDB:5YHG"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:5YHG"
FT HELIX 257..265
FT /evidence="ECO:0007829|PDB:5YHG"
FT STRAND 267..284
FT /evidence="ECO:0007829|PDB:5YHG"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:5YHG"
FT HELIX 296..303
FT /evidence="ECO:0007829|PDB:5YHG"
FT HELIX 308..314
FT /evidence="ECO:0007829|PDB:5YHG"
FT TURN 315..318
FT /evidence="ECO:0007829|PDB:5YH5"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:5YH5"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:5YHG"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:5YHG"
FT HELIX 345..354
FT /evidence="ECO:0007829|PDB:5YHG"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:5YHE"
FT STRAND 374..380
FT /evidence="ECO:0007829|PDB:5YHG"
FT HELIX 384..399
FT /evidence="ECO:0007829|PDB:5YHG"
FT STRAND 403..409
FT /evidence="ECO:0007829|PDB:5YHG"
FT HELIX 411..420
FT /evidence="ECO:0007829|PDB:5YHG"
FT STRAND 424..429
FT /evidence="ECO:0007829|PDB:5YHG"
FT TURN 433..437
FT /evidence="ECO:0007829|PDB:5YHG"
FT HELIX 438..442
FT /evidence="ECO:0007829|PDB:5YHG"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:5YHG"
FT TURN 447..450
FT /evidence="ECO:0007829|PDB:5YHG"
FT HELIX 451..454
FT /evidence="ECO:0007829|PDB:5YHG"
FT HELIX 460..470
FT /evidence="ECO:0007829|PDB:5YHG"
FT HELIX 476..493
FT /evidence="ECO:0007829|PDB:5YHG"
FT STRAND 496..509
FT /evidence="ECO:0007829|PDB:5YHG"
FT TURN 526..528
FT /evidence="ECO:0007829|PDB:5YHG"
SQ SEQUENCE 532 AA; 60077 MW; 52D6A60083052E70 CRC64;
MRKLTKMSAM LLASGLILTG CGGNKGLEEK KENKQLTYTT VKDIGDMNPH VYGGSMSAES
MIYEPLVRNT KDGIKPLLAK KWDVSEDGKT YTFHLRDDVK FHDGTPFDAD AVKKNIDAVQ
ENKKLHSWLK 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 IAAFKEKNGY ESATSGIENK DKIYNSIDDA FKIQNGKERS
DAYKNILKQI DDEGIFIPIS HGSMTVVAPK DLEKVSFTQS QYELPFNEMQ YK
