(data stored in ACNUC7421 zone)

SWISSPROT: ZNUB_BACSU

ID   ZNUB_BACSU              Reviewed;         280 AA.
AC   O34610; Q797R4;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   11-DEC-2019, entry version 107.
DE   RecName: Full=High-affinity zinc uptake system membrane protein ZnuB;
GN   Name=znuB; Synonyms=adcB, yceA; OrderedLocusNames=BSU02870;
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, AND INDUCTION.
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   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).
CC   -!- FUNCTION: Part of the high-affinity ABC transporter complex ZnuABC
CC       involved in zinc import (Probable). Responsible for the translocation
CC       of the substrate across the membrane (By similarity). ZnuABC-mediated
CC       zinc transport is required for comF expression and competence
CC       development. {ECO:0000250, ECO:0000269|PubMed:21813502,
CC       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:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- INDUCTION: Repressed by zinc via the metallo-regulatory protein Zur.
CC       {ECO:0000269|PubMed:12426338, ECO:0000269|PubMed:9811636}.
CC   -!- DISRUPTION PHENOTYPE: Disruption results in low transformability.
CC       {ECO:0000269|PubMed:21813502}.
CC   -!- SIMILARITY: Belongs to the ABC-3 integral membrane protein family.
CC       {ECO:0000305}.
DR   EMBL; AB000617; BAA22248.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12081.1; -; Genomic_DNA.
DR   PIR; C69756; C69756.
DR   RefSeq; NP_388169.1; NC_000964.3.
DR   RefSeq; WP_003246340.1; NZ_JNCM01000030.1.
DR   STRING; 224308.BSU02870; -.
DR   TCDB; 3.A.1.15.11; the atp-binding cassette (abc) superfamily.
DR   PaxDb; O34610; -.
DR   PRIDE; O34610; -.
DR   EnsemblBacteria; CAB12081; CAB12081; BSU02870.
DR   GeneID; 938367; -.
DR   KEGG; bsu:BSU02870; -.
DR   PATRIC; fig|224308.179.peg.298; -.
DR   eggNOG; COG1108; LUCA.
DR   HOGENOM; HOG000181429; -.
DR   InParanoid; O34610; -.
DR   KO; K09816; -.
DR   OMA; PMAMLSC; -.
DR   PhylomeDB; O34610; -.
DR   BioCyc; BSUB:BSU02870-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0010043; P:response to zinc ion; IBA:GO_Central.
DR   GO; GO:0006829; P:zinc ion transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3470.10; -; 1.
DR   InterPro; IPR037294; ABC_BtuC-like.
DR   InterPro; IPR001626; ABC_TroCD.
DR   PANTHER; PTHR30477; PTHR30477; 1.
DR   Pfam; PF00950; ABC-3; 1.
DR   SUPFAM; SSF81345; SSF81345; 1.
PE   1: Evidence at protein level;
DR   PRODOM; O34610.
DR   SWISS-2DPAGE; O34610.
KW   Cell membrane; Ion transport; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Zinc; Zinc transport.
FT   CHAIN           1..280
FT                   /note="High-affinity zinc uptake system membrane protein
FT                   ZnuB"
FT                   /id="PRO_0000360807"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        214..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   280 AA;  30436 MW;  CDB80E779D840426 CRC64;
     MEMFDLEFMR RAFLAGGMIA VMAPILGVYL VLRRQALMAD TLSHISLSGV AIGFFLSTNI
     TAASIVVVTI GAIGIEYMRR AYRTYSEVSI AILMAAGLSF AMFLISLSKG TANMSIDQYL
     FGSLVTVNQQ QVYIISIITL LILLYFIVLR RPLYLLTFDE ATAKTSGINT NVLSLSFSIV
     TGLAISVIIP IIGVLLVSAL LVLPAAFAIR IAKGFNMVFI TAILISLFSV FTGLTSSYQL
     GTPPGPSITL LLIVLLLIGF AVQGVWTFIK KEAQRKKRSR
//

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