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Database: UniProt
Entry: ZNUA_BRUA2
LinkDB: ZNUA_BRUA2
Original site: ZNUA_BRUA2 
ID   ZNUA_BRUA2              Reviewed;         334 AA.
AC   Q2YJH5; Q58J93;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=High-affinity zinc uptake system protein ZnuA;
DE   Flags: Precursor;
GN   Name=znuA; OrderedLocusNames=BAB2_1079;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16790759; DOI=10.1128/iai.01957-05;
RA   Yang X., Becker T., Walters N., Pascual D.W.;
RT   "Deletion of znuA virulence factor attenuates Brucella abortus and confers
RT   protection against wild-type challenge.";
RL   Infect. Immun. 74:3874-3879(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
CC   -!- FUNCTION: Part of the ATP-binding cassette (ABC) transport system
CC       ZnuABC involved in zinc import (PubMed:16790759). Binds zinc with high
CC       affinity and specificity and delivers it to the membrane permease for
CC       translocation into the cytoplasm (PubMed:16790759). Required for
CC       survival and normal growth under low Zn (2+) concentrations
CC       (PubMed:16790759). Also required for virulence and intracellular growth
CC       in macrophages (PubMed:16790759). {ECO:0000269|PubMed:16790759}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:A1B9L0}.
CC   -!- DISRUPTION PHENOTYPE: Mutant strain (znuA delection) is attenuated in
CC       infected mice, showing decreased splenic CFU. Also confers a protective
CC       efficacy similar to that of RB51 and S19 vaccine strains.
CC       {ECO:0000269|PubMed:16790759}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 9 family.
CC       {ECO:0000305}.
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DR   EMBL; AY941821; AAX46323.1; -; Genomic_DNA.
DR   EMBL; AM040265; CAJ13245.1; -; Genomic_DNA.
DR   RefSeq; WP_002966661.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YJH5; -.
DR   SMR; Q2YJH5; -.
DR   STRING; 359391.BAB2_1079; -.
DR   GeneID; 3827700; -.
DR   KEGG; bmf:BAB2_1079; -.
DR   PATRIC; fig|359391.11.peg.1863; -.
DR   HOGENOM; CLU_016838_1_2_5; -.
DR   PhylomeDB; Q2YJH5; -.
DR   PRO; PR:Q2YJH5; -.
DR   Proteomes; UP000002719; Chromosome II.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006829; P:zinc ion transport; IEA:UniProtKB-KW.
DR   CDD; cd01019; ZnuA; 1.
DR   Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2.
DR   InterPro; IPR035520; ZnuA.
DR   InterPro; IPR006127; ZnuA-like.
DR   PANTHER; PTHR42953:SF3; HIGH-AFFINITY ZINC UPTAKE SYSTEM PROTEIN ZNUA; 1.
DR   PANTHER; PTHR42953; HIGH-AFFINITY ZINC UPTAKE SYSTEM PROTEIN ZNUA-RELATED; 1.
DR   Pfam; PF01297; ZnuA; 1.
DR   SUPFAM; SSF53807; Helical backbone' metal receptor; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Ion transport; Metal-binding; Periplasm;
KW   Reference proteome; Signal; Transport; Virulence; Zinc; Zinc transport.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..334
FT                   /note="High-affinity zinc uptake system protein ZnuA"
FT                   /id="PRO_0000248947"
FT   REGION          120..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P39172"
FT   BINDING         61
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P39172"
FT   BINDING         168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P39172"
FT   BINDING         232
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P39172"
FT   DISULFID        277..331
FT                   /evidence="ECO:0000250|UniProtKB:P39172"
FT   CONFLICT        266
FT                   /note="I -> T (in Ref. 1; AAX46323)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   334 AA;  36046 MW;  F3C873631569099F CRC64;
     MKNLHSLFLA SAFLAGFCGS SLAGEREGVV VSIKPLHSIV SAVMQGVGKP KLIVQGAGSE
     HVYSLKPSDA EAIEHAKVIF WAGPSMETFL DKPIDTLGEG AKVVALGDAK GLTKLKFREG
     GPFEAHDHGH GGSHEEEHDA HGSGDHDHAA EVAEEGHEHH HHGEYDLHFW LDPQNGKILA
     ADIAKTLGES DPEHAAQYEK NAKAYGEKLD ALTREVAAEL KPVKDKPFIV FHDAYQYFEN
     RFGMKAAGSI TVSPEKAPGA ARIQQIHDKI KSLGATCVFS EPQFEPKLVK TVVDGTKART
     GVLDPLGAEL KDGPDLYPQL IRNLANSLKD CLPK
//
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