NIKA_ECOLI
ID NIKA_ECOLI Reviewed; 524 AA.
AC P33590; Q2M7D9;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Nickel-binding periplasmic protein;
DE Flags: Precursor;
GN Name=nikA; OrderedLocusNames=b3476, JW3441;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=7934931; DOI=10.1111/j.1365-2958.1993.tb01247.x;
RA Navarro C., Wu L.-F., Mandrand-Berthelot M.-A.;
RT "The nik operon of Escherichia coli encodes a periplasmic binding-protein-
RT dependent transport system for nickel.";
RL Mol. Microbiol. 9:1181-1191(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 23-524.
RX PubMed=12960164; DOI=10.1074/jbc.m307941200;
RA Heddle J., Scott D.J., Unzai S., Park S.Y., Tame J.R.;
RT "Crystal structures of the liganded and unliganded nickel-binding protein
RT NikA from Escherichia coli.";
RL J. Biol. Chem. 278:50322-50329(2003).
CC -!- FUNCTION: Involved in a nickel transport system, probably represents
CC the nickel binder.
CC -!- INTERACTION:
CC P33590; P0CE47: tufA; NbExp=2; IntAct=EBI-555182, EBI-301077;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC {ECO:0000305}.
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DR EMBL; X73143; CAA51659.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18451.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76501.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77817.1; -; Genomic_DNA.
DR PIR; S39594; S39594.
DR RefSeq; NP_417933.1; NC_000913.3.
DR RefSeq; WP_000953361.1; NZ_SSZK01000008.1.
DR PDB; 1UIU; X-ray; 1.85 A; A/B=23-524.
DR PDB; 1UIV; X-ray; 1.95 A; A/B=23-524.
DR PDB; 1ZLQ; X-ray; 1.80 A; A/B=23-524.
DR PDB; 2NOO; X-ray; 1.65 A; A=23-524.
DR PDB; 3DP8; X-ray; 2.50 A; A/B/C=23-524.
DR PDB; 3E3K; X-ray; 2.80 A; A/B/C=23-524.
DR PDB; 3MVW; X-ray; 1.79 A; A/B=23-524.
DR PDB; 3MVX; X-ray; 1.70 A; A/B=23-524.
DR PDB; 3MVY; X-ray; 2.50 A; A/B=23-524.
DR PDB; 3MVZ; X-ray; 1.70 A; A/B=23-524.
DR PDB; 3MW0; X-ray; 2.30 A; A/B=23-524.
DR PDB; 3MZ9; X-ray; 1.80 A; A/B=23-524.
DR PDB; 3MZB; X-ray; 1.70 A; A/B=23-523.
DR PDB; 3QIM; X-ray; 2.10 A; A/B=23-524.
DR PDB; 4DCX; X-ray; 2.00 A; A/B=23-524.
DR PDB; 4DCY; X-ray; 2.00 A; A/B=23-524.
DR PDB; 4I8C; X-ray; 2.50 A; A/B/C=23-524.
DR PDB; 4I9D; X-ray; 1.70 A; A/B=23-524.
DR PDB; 5L8D; X-ray; 1.80 A; A/B=23-524.
DR PDB; 5MWU; X-ray; 1.80 A; A/B=23-524.
DR PDB; 5ON0; X-ray; 1.90 A; A/B=23-524.
DR PDB; 5ON1; X-ray; 1.70 A; A/B=23-524.
DR PDB; 5ON4; X-ray; 2.30 A; A/B=23-524.
DR PDB; 5ON5; X-ray; 1.70 A; A/B=23-524.
DR PDB; 5ON8; X-ray; 1.60 A; A/B=23-524.
DR PDB; 5ON9; X-ray; 1.70 A; A/B=23-524.
DR PDB; 6R4Q; X-ray; 1.90 A; A/B=23-524.
DR PDB; 7A0C; X-ray; 1.90 A; A/B=23-524.
DR PDBsum; 1UIU; -.
DR PDBsum; 1UIV; -.
DR PDBsum; 1ZLQ; -.
DR PDBsum; 2NOO; -.
DR PDBsum; 3DP8; -.
DR PDBsum; 3E3K; -.
DR PDBsum; 3MVW; -.
DR PDBsum; 3MVX; -.
DR PDBsum; 3MVY; -.
DR PDBsum; 3MVZ; -.
DR PDBsum; 3MW0; -.
DR PDBsum; 3MZ9; -.
DR PDBsum; 3MZB; -.
DR PDBsum; 3QIM; -.
DR PDBsum; 4DCX; -.
DR PDBsum; 4DCY; -.
DR PDBsum; 4I8C; -.
DR PDBsum; 4I9D; -.
DR PDBsum; 5L8D; -.
DR PDBsum; 5MWU; -.
DR PDBsum; 5ON0; -.
DR PDBsum; 5ON1; -.
DR PDBsum; 5ON4; -.
DR PDBsum; 5ON5; -.
DR PDBsum; 5ON8; -.
DR PDBsum; 5ON9; -.
DR PDBsum; 6R4Q; -.
DR PDBsum; 7A0C; -.
DR AlphaFoldDB; P33590; -.
DR BMRB; P33590; -.
DR SMR; P33590; -.
DR BioGRID; 4262491; 49.
DR ComplexPortal; CPX-4348; Nickel ABC transporter complex.
DR DIP; DIP-10340N; -.
DR IntAct; P33590; 1.
DR STRING; 511145.b3476; -.
DR DrugBank; DB03374; 3,5-Diiodotyrosine.
DR TCDB; 3.A.1.5.3; the atp-binding cassette (abc) superfamily.
DR jPOST; P33590; -.
DR PaxDb; P33590; -.
DR PRIDE; P33590; -.
DR EnsemblBacteria; AAC76501; AAC76501; b3476.
DR EnsemblBacteria; BAE77817; BAE77817; BAE77817.
DR GeneID; 947981; -.
DR KEGG; ecj:JW3441; -.
DR KEGG; eco:b3476; -.
DR PATRIC; fig|1411691.4.peg.3249; -.
DR EchoBASE; EB2000; -.
DR eggNOG; COG0747; Bacteria.
DR HOGENOM; CLU_017028_7_5_6; -.
DR InParanoid; P33590; -.
DR OMA; YIPLTYQ; -.
DR PhylomeDB; P33590; -.
DR BioCyc; EcoCyc:NIKA-MON; -.
DR BioCyc; MetaCyc:NIKA-MON; -.
DR EvolutionaryTrace; P33590; -.
DR PRO; PR:P33590; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0042597; C:periplasmic space; IDA:EcoliWiki.
DR GO; GO:0020037; F:heme binding; IDA:EcoliWiki.
DR GO; GO:0051540; F:metal cluster binding; IDA:EcoCyc.
DR GO; GO:0016151; F:nickel cation binding; IDA:EcoliWiki.
DR GO; GO:1904680; F:peptide transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046914; F:transition metal ion binding; IDA:EcoliWiki.
DR GO; GO:0050919; P:negative chemotaxis; IMP:EcoliWiki.
DR GO; GO:0098716; P:nickel cation import across plasma membrane; IC:ComplexPortal.
DR GO; GO:0015833; P:peptide transport; IBA:GO_Central.
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; PS01040; SBP_BACTERIAL_5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nickel; Periplasm; Reference proteome; Signal; Transport.
FT SIGNAL 1..22
FT CHAIN 23..524
FT /note="Nickel-binding periplasmic protein"
FT /id="PRO_0000031800"
FT STRAND 27..34
FT /evidence="ECO:0007829|PDB:5ON8"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:2NOO"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:5ON8"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:5ON8"
FT STRAND 68..78
FT /evidence="ECO:0007829|PDB:5ON8"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1UIU"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:5ON8"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:3DP8"
FT HELIX 103..114
FT /evidence="ECO:0007829|PDB:5ON8"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:5ON8"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:5ON8"
FT STRAND 129..146
FT /evidence="ECO:0007829|PDB:5ON8"
FT HELIX 151..155
FT /evidence="ECO:0007829|PDB:5ON8"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:5ON8"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:5ON8"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1UIV"
FT STRAND 173..180
FT /evidence="ECO:0007829|PDB:5ON8"
FT STRAND 184..193
FT /evidence="ECO:0007829|PDB:5ON8"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:5ON8"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:5ON8"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:5ON8"
FT HELIX 224..232
FT /evidence="ECO:0007829|PDB:5ON8"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:3E3K"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:5ON8"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:2NOO"
FT HELIX 248..256
FT /evidence="ECO:0007829|PDB:5ON8"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:5ON8"
FT STRAND 269..275
FT /evidence="ECO:0007829|PDB:5ON8"
FT TURN 280..283
FT /evidence="ECO:0007829|PDB:5ON8"
FT HELIX 285..294
FT /evidence="ECO:0007829|PDB:5ON8"
FT HELIX 297..304
FT /evidence="ECO:0007829|PDB:5ON8"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:2NOO"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:5ON8"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:5ON8"
FT HELIX 334..343
FT /evidence="ECO:0007829|PDB:5ON8"
FT STRAND 363..369
FT /evidence="ECO:0007829|PDB:5ON8"
FT HELIX 373..387
FT /evidence="ECO:0007829|PDB:5ON8"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:5ON8"
FT STRAND 392..398
FT /evidence="ECO:0007829|PDB:5ON8"
FT HELIX 400..409
FT /evidence="ECO:0007829|PDB:5ON8"
FT STRAND 413..418
FT /evidence="ECO:0007829|PDB:5ON8"
FT TURN 422..426
FT /evidence="ECO:0007829|PDB:5ON8"
FT HELIX 427..432
FT /evidence="ECO:0007829|PDB:5ON8"
FT STRAND 435..438
FT /evidence="ECO:0007829|PDB:2NOO"
FT HELIX 439..444
FT /evidence="ECO:0007829|PDB:5ON8"
FT HELIX 450..461
FT /evidence="ECO:0007829|PDB:5ON8"
FT HELIX 466..482
FT /evidence="ECO:0007829|PDB:5ON8"
FT STRAND 486..492
FT /evidence="ECO:0007829|PDB:5ON8"
FT STRAND 495..498
FT /evidence="ECO:0007829|PDB:5ON8"
FT HELIX 500..502
FT /evidence="ECO:0007829|PDB:5ON8"
FT HELIX 516..518
FT /evidence="ECO:0007829|PDB:5ON8"
SQ SEQUENCE 524 AA; 58719 MW; CB2E3C1CDCE42396 CRC64;
MLSTLRRTLF ALLACASFIV HAAAPDEITT AWPVNVGPLN PHLYTPNQMF AQSMVYEPLV
KYQADGSVIP WLAKSWTHSE DGKTWTFTLR DDVKFSNGEP FDAEAAAENF RAVLDNRQRH
AWLELANQIV DVKALSKTEL QITLKSAYYP FLQELALPRP FRFIAPSQFK NHETMNGIKA
PIGTGPWILQ ESKLNQYDVF VRNENYWGEK PAIKKITFNV IPDPTTRAVA FETGDIDLLY
GNEGLLPLDT FARFSQNPAY HTQLSQPIET VMLALNTAKA PTNELAVREA LNYAVNKKSL
IDNALYGTQQ VADTLFAPSV PYANLGLKPS QYDPQKAKAL LEKAGWTLPA GKDIREKNGQ
PLRIELSFIG TDALSKSMAE IIQADMRQIG ADVSLIGEEE SSIYARQRDG RFGMIFHRTW
GAPYDPHAFL SSMRVPSHAD FQAQQGLADK PLIDKEIGEV LATHDETQRQ ALYRDILTRL
HDEAVYLPIS YISMMVVSKP ELGNIPYAPI ATEIPFEQIK PVKP
