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 03-AUG-2022, entry version 115.
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; 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 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}.
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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 AlphaFoldDB; O34610; -.
DR SMR; O34610; -.
DR STRING; 224308.BSU02870; -.
DR TCDB; 3.A.1.15.11; the atp-binding cassette (abc) superfamily.
DR PaxDb; O34610; -.
DR EnsemblBacteria; CAB12081; CAB12081; BSU_02870.
DR GeneID; 938367; -.
DR KEGG; bsu:BSU02870; -.
DR PATRIC; fig|224308.179.peg.298; -.
DR eggNOG; COG1108; Bacteria.
DR InParanoid; O34610; -.
DR OMA; ALMGDGI; -.
DR PhylomeDB; O34610; -.
DR BioCyc; BSUB:BSU02870-MON; -.
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:0010043; P:response to zinc ion; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
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;
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
