NIKA_STAA8
ID NIKA_STAA8 Reviewed; 491 AA.
AC Q2G2P5; A0A0H2UKY7; A0A0J9X272;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-JUN-2019, sequence version 2.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Nickel-binding protein NikA {ECO:0000305};
DE AltName: Full=SaNikA {ECO:0000303|PubMed:25611161};
DE Flags: Precursor;
GN Name=nikA {ECO:0000303|PubMed:20662775};
GN Synonyms=opp5A {ECO:0000303|PubMed:20662775};
GN OrderedLocusNames=SAOUHSC_00201 {ECO:0000312|EMBL:ABD29379.1};
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 FUNCTION, SUBUNIT, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=RN6390;
RX PubMed=20662775; DOI=10.1111/j.1365-2958.2010.07287.x;
RA Hiron A., Posteraro B., Carriere M., Remy L., Delporte C., La Sorda M.,
RA Sanguinetti M., Juillard V., Borezee-Durant E.;
RT "A nickel ABC-transporter of Staphylococcus aureus is involved in urinary
RT tract infection.";
RL Mol. Microbiol. 77:1246-1260(2010).
RN [3] {ECO:0007744|PDB:3RQT}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 23-491.
RA Minasov G., Halavaty A., Shuvalova L., Dubrovska I., Winsor J.,
RA Kiryukhina O., Falugi F., Bottomley M., Bagnoli F., Grandi G.,
RA Anderson W.F.;
RT "1.5 angstrom crystal structure of the complex of ligand binding component
RT of ABC-type import system from Staphylococcus aureus with nickel and two
RT histidines.";
RL Submitted (APR-2011) to the PDB data bank.
RN [4] {ECO:0007744|PDB:4OFJ, ECO:0007744|PDB:4XKN, ECO:0007744|PDB:4XKP, ECO:0007744|PDB:4XKQ, ECO:0007744|PDB:4XKR}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 22-491 IN COMPLEXES WITH NICKEL
RP AND FREE HISTIDINES, AND FUNCTION.
RC STRAIN=RN6390;
RX PubMed=25611161; DOI=10.1039/c4mt00295d;
RA Lebrette H., Borezee-Durant E., Martin L., Richaud P., Boeri Erba E.,
RA Cavazza C.;
RT "Novel insights into nickel import in Staphylococcus aureus: the positive
RT role of free histidine and structural characterization of a new
RT thiazolidine-type nickel chelator.";
RL Metallomics 7:613-621(2015).
CC -!- FUNCTION: Part of the ABC transporter complex NikABCDE (Opp2) involved
CC in nickel import. Binds nickel and transfers it to the membrane-bound
CC permease. Required for full urease activity and plays a significant
CC role in the virulence of S.aureus during urinary tract infection (UTI)
CC (PubMed:20662775). May bind nickel via a nickel-chelator
CC (PubMed:25611161). {ECO:0000269|PubMed:20662775,
CC ECO:0000269|PubMed:25611161}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (NikD and
CC NikE), two transmembrane proteins (NikB and NikC) and a solute-binding
CC protein (NikA). {ECO:0000269|PubMed:20662775}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- INDUCTION: Induced in response to decrease in pH and as a function of
CC growth phase. {ECO:0000269|PubMed:20662775}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene strongly reduces nickel
CC transport and urease activity. Mutant shows decreased virulence in a
CC mouse model of ascending UTI. Nickel accumulation and urease activity
CC are almost completely abolished in a nixA-nikA double mutant.
CC {ECO:0000269|PubMed:20662775}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABD29379.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000253; ABD29379.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000669653.1; NZ_LS483365.1.
DR RefSeq; YP_498798.1; NC_007795.1.
DR PDB; 3RQT; X-ray; 1.50 A; A=23-491.
DR PDB; 4OFJ; X-ray; 1.70 A; A=22-491.
DR PDB; 4XKN; X-ray; 1.85 A; A=22-491.
DR PDB; 4XKP; X-ray; 1.90 A; A=22-491.
DR PDB; 4XKQ; X-ray; 1.90 A; A=22-491.
DR PDB; 4XKR; X-ray; 1.75 A; A=22-491.
DR PDBsum; 3RQT; -.
DR PDBsum; 4OFJ; -.
DR PDBsum; 4XKN; -.
DR PDBsum; 4XKP; -.
DR PDBsum; 4XKQ; -.
DR PDBsum; 4XKR; -.
DR AlphaFoldDB; Q2G2P5; -.
DR SMR; Q2G2P5; -.
DR STRING; 1280.SAXN108_0215; -.
DR EnsemblBacteria; ABD29379; ABD29379; SAOUHSC_00201.
DR GeneID; 3920357; -.
DR KEGG; sao:SAOUHSC_00201; -.
DR PATRIC; fig|93061.5.peg.186; -.
DR eggNOG; COG0747; Bacteria.
DR HOGENOM; CLU_017028_7_5_9; -.
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:1904680; F:peptide transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015675; P:nickel cation transport; IEA:UniProtKB-KW.
DR GO; GO:0015833; P:peptide transport; IBA:GO_Central.
DR InterPro; IPR030678; Peptide/Ni-bd.
DR InterPro; IPR039424; SBP_5.
DR InterPro; IPR000914; SBP_5_dom.
DR PANTHER; PTHR30290; PTHR30290; 1.
DR Pfam; PF00496; SBP_bac_5; 1.
DR PIRSF; PIRSF002741; MppA; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Ion transport; Lipoprotein; Membrane; Nickel;
KW Nickel transport; Palmitate; Reference proteome; Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 19..491
FT /note="Nickel-binding protein NikA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT /id="PRO_0000447263"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:3RQT"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:3RQT"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:3RQT"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:3RQT"
FT STRAND 66..78
FT /evidence="ECO:0007829|PDB:3RQT"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:3RQT"
FT HELIX 100..113
FT /evidence="ECO:0007829|PDB:3RQT"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:3RQT"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:3RQT"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:3RQT"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:3RQT"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:3RQT"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:3RQT"
FT STRAND 171..180
FT /evidence="ECO:0007829|PDB:3RQT"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:3RQT"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:3RQT"
FT STRAND 201..207
FT /evidence="ECO:0007829|PDB:3RQT"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:3RQT"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:3RQT"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:3RQT"
FT HELIX 234..239
FT /evidence="ECO:0007829|PDB:3RQT"
FT STRAND 243..258
FT /evidence="ECO:0007829|PDB:3RQT"
FT HELIX 267..276
FT /evidence="ECO:0007829|PDB:3RQT"
FT HELIX 279..285
FT /evidence="ECO:0007829|PDB:3RQT"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:3RQT"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:3RQT"
FT HELIX 315..323
FT /evidence="ECO:0007829|PDB:3RQT"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:3RQT"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:3RQT"
FT STRAND 333..339
FT /evidence="ECO:0007829|PDB:3RQT"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:3RQT"
FT HELIX 345..358
FT /evidence="ECO:0007829|PDB:3RQT"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:3RQT"
FT STRAND 362..368
FT /evidence="ECO:0007829|PDB:3RQT"
FT HELIX 372..375
FT /evidence="ECO:0007829|PDB:3RQT"
FT STRAND 383..391
FT /evidence="ECO:0007829|PDB:3RQT"
FT HELIX 398..404
FT /evidence="ECO:0007829|PDB:3RQT"
FT HELIX 419..429
FT /evidence="ECO:0007829|PDB:3RQT"
FT HELIX 434..451
FT /evidence="ECO:0007829|PDB:3RQT"
FT STRAND 453..467
FT /evidence="ECO:0007829|PDB:3RQT"
SQ SEQUENCE 491 AA; 55431 MW; FEA37FE7A00477E6 CRC64;
MKFKRLATIF SAVLVLSGCG SMHSSGKDLN ISLPLKTKSI APYETDVPVK IGAAESLFKT
NDQGKIEKAL VKSYHQPNDT TLDIELKDNI KFQNGQKLTA EKVKSSLENS MKKSDLVKYS
LPISSITAKG QKLTIKTNSA YPELVSELAN PFMAIYDTDA KSDVNQTPVG TGPYQIKDYK
QSRKISLSNF KDYWQGKPKL DHITVTYQED GNNRVRNLES QKDDLITDVP VNKVQDIENN
QNLKVSKESG FRTSLLMYNH TNKKMTKSVR EALDHIIDRQ GIADHIYQGY AKPATSPFND
KIPYIKEPKL TKQNIEQAKM LLAKDGYTKE HPLKIKLITY DGRPELSKIA QVLQSDAKKA
NIEIDIKSVD DIEGYLKDRS AWDATMYSFG TIPRGDTGYF FNQAYKKDGA INKGDYNNSN
VDDLINQLNH TVDVKERHNI SNDIIKLSSR DVPNSYIAYN DQIVAANSKV KNYKVTPEGI
YLIDYRTTIE R
