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 03-AUG-2022, entry version 118.
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; DOI=10.1128/jb.180.22.5815-5821.1998;
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 SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=22882210; DOI=10.1111/j.1365-2958.2012.08205.x;
RA Yepes A., Schneider J., Mielich B., Koch G., Garcia-Betancur J.C.,
RA Ramamurthi K.S., Vlamakis H., Lopez D.;
RT "The biofilm formation defect of a Bacillus subtilis flotillin-defective
RT mutant involves the protease FtsH.";
RL Mol. Microbiol. 86:457-471(2012).
RN [8]
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:0000269|PubMed:22882210,
CC ECO:0000305|PubMed:14730579}; Lipid-anchor
CC {ECO:0000305|PubMed:14730579}. Membrane raft
CC {ECO:0000269|PubMed:22882210}; Lipid-anchor
CC {ECO:0000305|PubMed:14730579}. Note=Present in detergent-resistant
CC membrane (DRM) fractions that may be equivalent to eukaryotic membrane
CC rafts; these rafts include proteins involved in signaling, molecule
CC trafficking and protein secretion. {ECO:0000269|PubMed:22882210}.
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}.
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; 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 AlphaFoldDB; O34966; -.
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 DNASU; 938370; -.
DR EnsemblBacteria; CAB12079; CAB12079; BSU_02850.
DR GeneID; 938370; -.
DR KEGG; bsu:BSU02850; -.
DR PATRIC; fig|224308.179.peg.296; -.
DR eggNOG; COG0803; Bacteria.
DR InParanoid; O34966; -.
DR OMA; HAAYDYL; -.
DR PhylomeDB; O34966; -.
DR BioCyc; BSUB:BSU02850-MON; -.
DR EvolutionaryTrace; O34966; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
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;
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:0007829|PDB:2O1E"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:2O1E"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:2O1E"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:2O1E"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:2O1E"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:2O1E"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:2O1E"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:2O1E"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:2O1E"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:2O1E"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:2O1E"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:2O1E"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:2O1E"
FT HELIX 153..170
FT /evidence="ECO:0007829|PDB:2O1E"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:2O1E"
FT HELIX 175..201
FT /evidence="ECO:0007829|PDB:2O1E"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:2O1E"
FT HELIX 216..221
FT /evidence="ECO:0007829|PDB:2O1E"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:2O1E"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:2O1E"
FT HELIX 240..249
FT /evidence="ECO:0007829|PDB:2O1E"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:2O1E"
FT HELIX 266..274
FT /evidence="ECO:0007829|PDB:2O1E"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:2O1E"
FT HELIX 291..296
FT /evidence="ECO:0007829|PDB:2O1E"
FT HELIX 300..315
FT /evidence="ECO:0007829|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
