ZNUA_ECOLI
ID ZNUA_ECOLI Reviewed; 310 AA.
AC P39172; P76284;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 4.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=High-affinity zinc uptake system protein ZnuA;
DE Flags: Precursor;
GN Name=znuA; Synonyms=yebL, yzzP; OrderedLocusNames=b1857, JW5831;
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 / EMG2;
RA Robison K., O'Keeffe T., Church G.M.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
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 PROTEIN SEQUENCE OF 27-38.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP PROTEIN SEQUENCE OF 27-36.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.;
RL Submitted (FEB-1996) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 27-30.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [8]
RP CHARACTERIZATION.
RX PubMed=9680209; DOI=10.1046/j.1365-2958.1998.00883.x;
RA Patzer S.I., Hantke K.;
RT "The ZnuABC high-affinity zinc uptake system and its regulator Zur in
RT Escherichia coli.";
RL Mol. Microbiol. 28:1199-1210(1998).
RN [9]
RP INDUCTION.
RC STRAIN=BW21135;
RX PubMed=22196016; DOI=10.1016/j.jinorgbio.2011.11.022;
RA Hensley M.P., Gunasekera T.S., Easton J.A., Sigdel T.K., Sugarbaker S.A.,
RA Klingbeil L., Breece R.M., Tierney D.L., Crowder M.W.;
RT "Characterization of Zn(II)-responsive ribosomal proteins YkgM and L31 in
RT E. coli.";
RL J. Inorg. Biochem. 111:164-172(2012).
CC -!- FUNCTION: Involved in the high-affinity zinc uptake transport system.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- INDUCTION: Maximally induced 30 minutes under zinc-limiting conditions,
CC still induced in stationary phase. {ECO:0000269|PubMed:22196016}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 9 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA81030.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U38702; AAA81030.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC74927.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15665.2; -; Genomic_DNA.
DR PIR; A64948; A64948.
DR RefSeq; NP_416371.4; NC_000913.3.
DR RefSeq; WP_001300644.1; NZ_SSZK01000001.1.
DR PDB; 2OGW; X-ray; 1.83 A; A/B=1-310.
DR PDB; 2OSV; X-ray; 1.75 A; A/B=27-310.
DR PDB; 2PRS; X-ray; 1.70 A; A/B=27-310.
DR PDB; 2PS0; X-ray; 2.00 A; A/B=27-310.
DR PDB; 2PS3; X-ray; 2.47 A; A/B=27-310.
DR PDB; 2PS9; X-ray; 2.15 A; A/B=27-310.
DR PDBsum; 2OGW; -.
DR PDBsum; 2OSV; -.
DR PDBsum; 2PRS; -.
DR PDBsum; 2PS0; -.
DR PDBsum; 2PS3; -.
DR PDBsum; 2PS9; -.
DR AlphaFoldDB; P39172; -.
DR SMR; P39172; -.
DR BioGRID; 4260353; 42.
DR ComplexPortal; CPX-4407; Zinc ABC transporter complex.
DR DIP; DIP-12949N; -.
DR STRING; 511145.b1857; -.
DR TCDB; 3.A.1.15.5; the atp-binding cassette (abc) superfamily.
DR SWISS-2DPAGE; P39172; -.
DR jPOST; P39172; -.
DR PaxDb; P39172; -.
DR PRIDE; P39172; -.
DR EnsemblBacteria; AAC74927; AAC74927; b1857.
DR EnsemblBacteria; BAA15665; BAA15665; BAA15665.
DR GeneID; 58462243; -.
DR GeneID; 946375; -.
DR KEGG; ecj:JW5831; -.
DR KEGG; eco:b1857; -.
DR PATRIC; fig|511145.12.peg.1936; -.
DR EchoBASE; EB2543; -.
DR eggNOG; COG4531; Bacteria.
DR HOGENOM; CLU_016838_1_2_6; -.
DR InParanoid; P39172; -.
DR OMA; FHEAFDY; -.
DR PhylomeDB; P39172; -.
DR BioCyc; EcoCyc:ZNUA-MON; -.
DR BioCyc; MetaCyc:ZNUA-MON; -.
DR EvolutionaryTrace; P39172; -.
DR PRO; PR:P39172; -.
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:0042597; C:periplasmic space; ISM:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0055069; P:zinc ion homeostasis; IC:ComplexPortal.
DR GO; GO:0071578; P:zinc ion import across plasma membrane; IC:ComplexPortal.
DR GO; GO:0006829; P:zinc ion transport; IDA:EcoCyc.
DR CDD; cd01019; ZnuA; 1.
DR InterPro; IPR006128; Lipoprotein_4.
DR InterPro; IPR035520; ZnuA.
DR InterPro; IPR006127; ZnuA-like.
DR Pfam; PF01297; ZnuA; 1.
DR PRINTS; PR00690; ADHESNFAMILY.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Ion transport; Metal-binding;
KW Periplasm; Reference proteome; Signal; Transport; Zinc; Zinc transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:9298646,
FT ECO:0000269|PubMed:9600841, ECO:0000269|Ref.6"
FT CHAIN 27..310
FT /note="High-affinity zinc uptake system protein ZnuA"
FT /id="PRO_0000031875"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CONFLICT 195
FT /note="L -> V (in Ref. 1; AAA81030)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="A -> P (in Ref. 1; AAA81030)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="K -> E (in Ref. 1; AAA81030)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="C -> S (in Ref. 1; AAA81030)"
FT /evidence="ECO:0000305"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:2PRS"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:2PRS"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:2PRS"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:2PRS"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:2PS3"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:2PRS"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:2PRS"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:2PRS"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:2PRS"
FT HELIX 90..94
FT /evidence="ECO:0007829|PDB:2PRS"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:2PRS"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:2PRS"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:2PRS"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:2PRS"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:2PRS"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:2PRS"
FT HELIX 148..165
FT /evidence="ECO:0007829|PDB:2PRS"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:2PRS"
FT HELIX 170..195
FT /evidence="ECO:0007829|PDB:2PRS"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:2PRS"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:2PRS"
FT HELIX 211..217
FT /evidence="ECO:0007829|PDB:2PRS"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:2PRS"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:2PS9"
FT HELIX 235..247
FT /evidence="ECO:0007829|PDB:2PRS"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:2PRS"
FT HELIX 262..267
FT /evidence="ECO:0007829|PDB:2PRS"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:2PRS"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:2PRS"
FT HELIX 291..307
FT /evidence="ECO:0007829|PDB:2PRS"
SQ SEQUENCE 310 AA; 33777 MW; 99500F04C6C3DBF0 CRC64;
MLHKKTLLFA ALSAALWGGA TQAADAAVVA SLKPVGFIAS AIADGVTETE VLLPDGASEH
DYSLRPSDVK RLQNADLVVW VGPEMEAFMQ KPVSKLPGAK QVTIAQLEDV KPLLMKSIHG
DDDDHDHAEK SDEDHHHGDF NMHLWLSPEI ARATAVAIHG KLVELMPQSR AKLDANLKDF
EAQLASTETQ VGNELAPLKG KGYFVFHDAY GYFEKQFGLT PLGHFTVNPE IQPGAQRLHE
IRTQLVEQKA TCVFAEPQFR PAVVESVARG TSVRMGTLDP LGTNIKLGKT SYSEFLSQLA
NQYASCLKGD
