(data stored in SCRATCH zone)

SWISSPROT: ZNUA_BACSU

ID   ZNUA_BACSU              Reviewed;         319 AA.
AC   O34966; Q797R6;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   11-DEC-2019, entry version 109.
DE   RecName: Full=High-affinity zinc uptake system binding-protein ZnuA;
DE   Flags: Precursor;
GN   Name=znuA; Synonyms=adcA, ycdH; OrderedLocusNames=BSU02850;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9274031; DOI=10.1099/00221287-143-8-2775;
RA   Kumano M., Tamakoshi A., Yamane K.;
RT   "A 32 kb nucleotide sequence from the region of the lincomycin-resistance
RT   gene (22 degrees-25 degrees) of the Bacillus subtilis chromosome and
RT   identification of the site of the lin-2 mutation.";
RL   Microbiology 143:2775-2782(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=9811636;
RA   Gaballa A., Helmann J.D.;
RT   "Identification of a zinc-specific metalloregulatory protein, Zur,
RT   controlling zinc transport operons in Bacillus subtilis.";
RL   J. Bacteriol. 180:5815-5821(1998).
RN   [4]
RP   INDUCTION.
RC   STRAIN=168;
RX   PubMed=12426338; DOI=10.1128/jb.184.23.6508-6514.2002;
RA   Gaballa A., Wang T., Ye R.W., Helmann J.D.;
RT   "Functional analysis of the Bacillus subtilis Zur regulon.";
RL   J. Bacteriol. 184:6508-6514(2002).
RN   [5]
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=14730579; DOI=10.1002/elps.200305676;
RA   Bunai K., Ariga M., Inoue T., Nozaki M., Ogane S., Kakeshita H., Nemoto T.,
RA   Nakanishi H., Yamane K.;
RT   "Profiling and comprehensive expression analysis of ABC transporter solute-
RT   binding proteins of Bacillus subtilis membrane based on a proteomic
RT   approach.";
RL   Electrophoresis 25:141-155(2004).
RN   [6]
RP   FUNCTION IN COMPETENCE DEVELOPMENT, DISRUPTION PHENOTYPE, AND GENE NAME.
RC   STRAIN=168;
RX   PubMed=21813502; DOI=10.1093/jb/mvr098;
RA   Ogura M.;
RT   "ZnuABC and ZosA zinc transporters are differently involved in competence
RT   development in Bacillus subtilis.";
RL   J. Biochem. 150:615-625(2011).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 22-319.
RG   Northeast structural genomics consortium (NESG);
RT   "Crystal structure of the metal-dependent lipoprotein YcdH from Bacillus
RT   subtilis, northeast structural genomics target sr583.";
RL   Submitted (FEB-2009) to the PDB data bank.
CC   -!- FUNCTION: Part of the high-affinity ABC transporter complex ZnuABC
CC       involved in zinc import (Probable). ZnuABC-mediated zinc transport is
CC       required for comF expression and competence development.
CC       {ECO:0000269|PubMed:21813502, ECO:0000269|PubMed:9811636, ECO:0000305}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (ZnuC),
CC       two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA).
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:14730579};
CC       Lipid-anchor {ECO:0000305|PubMed:14730579}.
CC   -!- INDUCTION: Repressed by zinc via the metallo-regulatory protein Zur.
CC       {ECO:0000269|PubMed:12426338, ECO:0000269|PubMed:9811636}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene grow slowly in zinc-
CC       deficient medium; this effect is suppressed upon addition of exogenous
CC       Zn(2+). Growth is slower yet in a double knockout with YciC. Disruption
CC       results in low transformability. {ECO:0000269|PubMed:21813502,
CC       ECO:0000269|PubMed:9811636}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 9 family.
CC       {ECO:0000305}.
DR   EMBL; AB000617; BAA22246.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12079.1; -; Genomic_DNA.
DR   PIR; A69756; A69756.
DR   RefSeq; NP_388167.1; NC_000964.3.
DR   RefSeq; WP_003234733.1; NZ_JNCM01000030.1.
DR   PDB; 2O1E; X-ray; 2.60 A; A/B=22-319.
DR   PDBsum; 2O1E; -.
DR   SMR; O34966; -.
DR   STRING; 224308.BSU02850; -.
DR   TCDB; 3.A.1.15.11; the atp-binding cassette (abc) superfamily.
DR   PaxDb; O34966; -.
DR   PRIDE; O34966; -.
DR   EnsemblBacteria; CAB12079; CAB12079; BSU02850.
DR   GeneID; 938370; -.
DR   KEGG; bsu:BSU02850; -.
DR   PATRIC; fig|224308.179.peg.296; -.
DR   eggNOG; ENOG4105DSE; Bacteria.
DR   eggNOG; COG0803; LUCA.
DR   HOGENOM; HOG000180308; -.
DR   InParanoid; O34966; -.
DR   KO; K09815; -.
DR   OMA; HAAYDYL; -.
DR   PhylomeDB; O34966; -.
DR   BioCyc; BSUB:BSU02850-MONOMER; -.
DR   EvolutionaryTrace; O34966; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0006829; P:zinc ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR006129; AdhesinB.
DR   InterPro; IPR006128; Lipoprotein_4.
DR   InterPro; IPR006127; ZnuA-like.
DR   Pfam; PF01297; ZnuA; 1.
DR   PRINTS; PR00691; ADHESINB.
DR   PRINTS; PR00690; ADHESNFAMILY.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
DR   PRODOM; O34966.
DR   SWISS-2DPAGE; O34966.
KW   3D-structure; Cell membrane; Ion transport; Lipoprotein; Membrane;
KW   Palmitate; Reference proteome; Signal; Transport; Zinc; Zinc transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           21..319
FT                   /note="High-affinity zinc uptake system binding-protein
FT                   ZnuA"
FT                   /id="PRO_0000360809"
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   STRAND          37..43
FT                   /evidence="ECO:0000244|PDB:2O1E"
FT   HELIX           44..54
FT                   /evidence="ECO:0000244|PDB:2O1E"
FT   HELIX           55..57
FT                   /evidence="ECO:0000244|PDB:2O1E"
FT   STRAND          58..64
FT                   /evidence="ECO:0000244|PDB:2O1E"
FT   TURN            70..72
FT                   /evidence="ECO:0000244|PDB:2O1E"
FT   HELIX           77..85
FT                   /evidence="ECO:0000244|PDB:2O1E"
FT   STRAND          86..92
FT                   /evidence="ECO:0000244|PDB:2O1E"
FT   TURN            94..96
FT                   /evidence="ECO:0000244|PDB:2O1E"
FT   HELIX           100..105
FT                   /evidence="ECO:0000244|PDB:2O1E"
FT   STRAND          109..111
FT                   /evidence="ECO:0000244|PDB:2O1E"
FT   STRAND          113..116
FT                   /evidence="ECO:0000244|PDB:2O1E"
FT   TURN            117..120
FT                   /evidence="ECO:0000244|PDB:2O1E"
FT   HELIX           149..151
FT                   /evidence="ECO:0000244|PDB:2O1E"
FT   HELIX           153..170
FT                   /evidence="ECO:0000244|PDB:2O1E"
FT   HELIX           172..174
FT                   /evidence="ECO:0000244|PDB:2O1E"
FT   HELIX           175..201
FT                   /evidence="ECO:0000244|PDB:2O1E"
FT   STRAND          207..212
FT                   /evidence="ECO:0000244|PDB:2O1E"
FT   HELIX           216..221
FT                   /evidence="ECO:0000244|PDB:2O1E"
FT   STRAND          225..228
FT                   /evidence="ECO:0000244|PDB:2O1E"
FT   STRAND          234..236
FT                   /evidence="ECO:0000244|PDB:2O1E"
FT   HELIX           240..249
FT                   /evidence="ECO:0000244|PDB:2O1E"
FT   STRAND          257..259
FT                   /evidence="ECO:0000244|PDB:2O1E"
FT   HELIX           266..274
FT                   /evidence="ECO:0000244|PDB:2O1E"
FT   STRAND          279..281
FT                   /evidence="ECO:0000244|PDB:2O1E"
FT   HELIX           291..296
FT                   /evidence="ECO:0000244|PDB:2O1E"
FT   HELIX           300..315
FT                   /evidence="ECO:0000244|PDB:2O1E"
SQ   SEQUENCE   319 AA;  35660 MW;  C66128D4FDE94D1B CRC64;
     MFKKWSGLFV IAACFLLVAA CGNSSTKGSA DSKGDKLHVV TTFYPMYEFT KQIVKDKGDV
     DLLIPSSVEP HDWEPTPKDI ANIQDADLFV YNSEYMETWV PSAEKSMGQG HAVFVNASKG
     IDLMEGSEEE HEEHDHGEHE HSHAMDPHVW LSPVLAQKEV KNITAQIVKQ DPDNKEYYEK
     NSKEYIAKLQ DLDKLYRTTA KKAEKKEFIT QHTAFGYLAK EYGLKQVPIA GLSPDQEPSA
     ASLAKLKTYA KEHNVKVIYF EEIASSKVAD TLASEIGAKT EVLNTLEGLS KEEQDKGLGY
     IDIMKQNLDA LKDSLLVKS
//

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