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Arsenite resistance protein ArsB

 ARSB_BACSU              Reviewed;         346 AA.
P45946;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
07-JUL-2009, sequence version 2.
23-MAY-2018, entry version 114.
RecName: Full=Arsenite resistance protein ArsB;
Name=arsB; Synonyms=yqcL; OrderedLocusNames=BSU25790;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168 / JH642;
PubMed=7704261; DOI=10.1099/13500872-141-2-323;
Takemaru K., Mizuno M., Sato T., Takeuchi M., Kobayashi Y.;
"Complete nucleotide sequence of a skin element excised by DNA
rearrangement during sporulation in Bacillus subtilis.";
Microbiology 141:323-327(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168 / JH642;
PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
Kobayashi Y.;
"Systematic sequencing of the 283 kb 210 degrees-232 degrees region of
the Bacillus subtilis genome containing the skin element and many
sporulation genes.";
Microbiology 142:3103-3111(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[4]
SEQUENCE REVISION TO 152.
PubMed=19383706; DOI=10.1099/mic.0.027839-0;
Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G.,
Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
"From a consortium sequence to a unified sequence: the Bacillus
subtilis 168 reference genome a decade later.";
Microbiology 155:1758-1775(2009).
[5]
IDENTIFICATION.
PubMed=7489895; DOI=10.1016/0378-1119(95)00636-K;
Medigue C., Moszer I., Viari A., Danchin A.;
"Analysis of a Bacillus subtilis genome fragment using a co-operative
computer system prototype.";
Gene 165:GC37-GC51(1995).
[6]
ROLE IN ARSENIC RESISTANCE.
PubMed=9537360;
Sato T., Kobayashi Y.;
"The ars operon in the skin element of Bacillus subtilis confers
resistance to arsenate and arsenite.";
J. Bacteriol. 180:1655-1661(1998).
-!- FUNCTION: Seems to confer resistance to arsenite by allowing cells
to extrude this compound. Could be part of an arsenite extrusion
pump. {ECO:0000269|PubMed:9537360}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass
membrane protein {ECO:0000305}.
-!- MISCELLANEOUS: Deletion of the arsB gene results in both an
aresenite- and arsenate-sensitive phenotype in the absence of
IPTG.
-!- SIMILARITY: Belongs to the arsenical resistance-3 (ACR3) (TC
2.A.59) family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D32216; BAA06969.1; -; Genomic_DNA.
EMBL; D84432; BAA12433.1; -; Genomic_DNA.
EMBL; AL009126; CAB14520.2; -; Genomic_DNA.
PIR; B69950; B69950.
RefSeq; NP_390456.2; NC_000964.3.
RefSeq; WP_004398718.1; NZ_JNCM01000036.1.
ProteinModelPortal; P45946; -.
STRING; 224308.Bsubs1_010100014106; -.
TCDB; 2.A.59.1.2; the arsenical resistance-3 (acr3) family.
PaxDb; P45946; -.
PRIDE; P45946; -.
EnsemblBacteria; CAB14520; CAB14520; BSU25790.
GeneID; 937800; -.
KEGG; bsu:BSU25790; -.
PATRIC; fig|224308.179.peg.2803; -.
eggNOG; ENOG4105D6J; Bacteria.
eggNOG; COG0798; LUCA.
HOGENOM; HOG000112302; -.
InParanoid; P45946; -.
KO; K03325; -.
OMA; CTAMVLM; -.
PhylomeDB; P45946; -.
BioCyc; BSUB:BSU25790-MONOMER; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0015104; F:antimonite transmembrane transporter activity; IBA:GO_Central.
GO; GO:0015297; F:antiporter activity; IBA:GO_Central.
GO; GO:0015105; F:arsenite transmembrane transporter activity; IBA:GO_Central.
GO; GO:0015699; P:antimonite transport; IBA:GO_Central.
GO; GO:0015700; P:arsenite transport; IBA:GO_Central.
GO; GO:0046685; P:response to arsenic-containing substance; IEA:UniProtKB-KW.
Gene3D; 1.20.1530.20; -; 1.
InterPro; IPR004706; Arsenical-R_Acr3.
InterPro; IPR002657; BilAc:Na_symport/Acr3.
InterPro; IPR038770; Na+/solute_symporter_sf.
PANTHER; PTHR43057; PTHR43057; 1.
Pfam; PF01758; SBF; 1.
PIRSF; PIRSF005508; Acr3; 1.
TIGRFAMs; TIGR00832; acr3; 1.
3: Inferred from homology;
Arsenical resistance; Cell membrane; Complete proteome; Membrane;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 346 Arsenite resistance protein ArsB.
/FTId=PRO_0000201482.
TRANSMEM 13 33 Helical. {ECO:0000255}.
TRANSMEM 41 61 Helical. {ECO:0000255}.
TRANSMEM 82 102 Helical. {ECO:0000255}.
TRANSMEM 106 126 Helical. {ECO:0000255}.
TRANSMEM 140 160 Helical. {ECO:0000255}.
TRANSMEM 184 204 Helical. {ECO:0000255}.
TRANSMEM 216 236 Helical. {ECO:0000255}.
TRANSMEM 253 273 Helical. {ECO:0000255}.
TRANSMEM 285 307 Helical. {ECO:0000255}.
TRANSMEM 318 338 Helical. {ECO:0000255}.
CONFLICT 152 152 F -> S (in Ref. 1; BAA06969 and 2;
BAA12433). {ECO:0000305}.
SEQUENCE 346 AA; 38312 MW; 05739D0B768A8644 CRC64;
MKRLSFLDRY LTIWIFLAMA LGIGLGFIFP SFVGGLNKLQ VGTTSIPLAI GLVLMMYPPL
AKVRYEEIGR VFKDIKVLIL SLVQNWIIGP TLMFILAIIF LPDKPEYMIG LIMIGLARCI
AMVIVWNDLS KGDTEYAAGL VAFNSIFQML FFSVYAYIFV TVIPQWLGME GAVVNITMAE
VAKSVFIYLG VPFIAGMVTR YIFVKVKGKE WYEKVFIPKI SPITLIALLF TIIVMFSLKG
DVIVSLPLDV VRVAIPLLIY FVLMFFVSFF LGKKIGANYA VTTTLAFTAG SNNFELAIAV
AVGVFGIHSG AAFAAVIGPL VEVPVMIALV KVALWFQRKY FGSHSM


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