YHEI_BACSU
ID YHEI_BACSU Reviewed; 585 AA.
AC O07550; Q796W6;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Probable multidrug resistance ABC transporter ATP-binding/permease protein YheI;
DE EC=7.6.2.-;
GN Name=yheI; OrderedLocusNames=BSU09710;
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=9579061; DOI=10.1099/00221287-144-4-859;
RA Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA Venema G., Bron S.;
RT "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL Microbiology 144:859-875(1998).
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 OVEREXPRESSION.
RC STRAIN=168;
RX PubMed=16487324; DOI=10.1111/j.1574-6968.2006.00104.x;
RA Fukushima S., Yoshimura M., Chibazakura T., Sato T., Yoshikawa H.;
RT "The putative ABC transporter YheH/YheI is involved in the signalling
RT pathway that activates KinA during sporulation initiation.";
RL FEMS Microbiol. Lett. 256:90-97(2006).
RN [4]
RP FUNCTION AS A TRANSPORTER, ATPASE ACTIVITY, ACTIVITY REGULATION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=168;
RX PubMed=19167342; DOI=10.1016/j.bbamem.2008.12.012;
RA Torres C., Galian C., Freiberg C., Fantino J.-R., Jault J.-M.;
RT "The YheI/YheH heterodimer from Bacillus subtilis is a multidrug ABC
RT transporter.";
RL Biochim. Biophys. Acta 1788:615-622(2009).
CC -!- FUNCTION: Involved in the transport of four structurally unrelated
CC drugs, including doxorubicin and mitoxantrone. Transmembrane domains
CC (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is
CC responsible for energy generation. {ECO:0000269|PubMed:19167342}.
CC -!- ACTIVITY REGULATION: Inhibited by ortho-vanadate.
CC {ECO:0000269|PubMed:19167342}.
CC -!- SUBUNIT: Heterodimer composed of YheH and YheI.
CC {ECO:0000269|PubMed:19167342}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19167342};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441,
CC ECO:0000269|PubMed:19167342}.
CC -!- INDUCTION: Induced by several classes of structurally unrelated
CC antibiotics, such as erythromycin, fusidic acid or linezolid.
CC {ECO:0000269|PubMed:19167342}.
CC -!- MISCELLANEOUS: Overexpression reduces the sporulation efficiency
CC possibly by modulating the function of KinA.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; Y14080; CAA74450.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12810.1; -; Genomic_DNA.
DR PIR; A69829; A69829.
DR RefSeq; NP_388852.1; NC_000964.3.
DR RefSeq; WP_003245157.1; NZ_JNCM01000035.1.
DR PDB; 7M33; EM; 3.55 A; C=2-585.
DR PDBsum; 7M33; -.
DR AlphaFoldDB; O07550; -.
DR SMR; O07550; -.
DR STRING; 224308.BSU09710; -.
DR TCDB; 3.A.1.106.8; the atp-binding cassette (abc) superfamily.
DR PaxDb; O07550; -.
DR PRIDE; O07550; -.
DR EnsemblBacteria; CAB12810; CAB12810; BSU_09710.
DR GeneID; 936278; -.
DR KEGG; bsu:BSU09710; -.
DR PATRIC; fig|224308.179.peg.1044; -.
DR eggNOG; COG1132; Bacteria.
DR InParanoid; O07550; -.
DR OMA; RYFEVMD; -.
DR PhylomeDB; O07550; -.
DR BioCyc; BSUB:BSU09710-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; ATP-binding; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..585
FT /note="Probable multidrug resistance ABC transporter ATP-
FT binding/permease protein YheI"
FT /id="PRO_0000376079"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 19..304
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 337..572
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 371..378
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 585 AA; 65112 MW; AB82FA64338F8161 CRC64;
MFSVLKKLGW FFKAYWLRYT IAIVLLLAVN VIEMFPPKLL GNAIDDMKAG AFTAEGLLFY
IGIFFVLTAA VYIMSYFWMH QLFGGANLME KILRTKLMGH LLTMSPPFYE KNRTGDLMAR
GTNDLQAVSL TTGFGILTLV DSTMFMMTIF LTMGFLISWK LTFAAIIPLP VMAIAISLYG
SKIHERFTEA QNAFGALNDR VLESVSGVRV IRAYVQETND VRRFNEMTAD VYQKNMKVAF
IDSLFEPTVK LLVGASYLIG LGYGAFLVFR NELTLGELVS FNVYLGMMIW PMFAIGELIN
VMQRGNASLD RVNETLSYET DVTDPKQPAD LKEPGDIVFS HVSFTYPSST SDNLQDISFT
VRKGQTVGIA GKTGSGKTTI IKQLLRQYPP GEGSITFSGV PIQQIPLDRL RGWIGYVPQD
HLLFSRTVKE NILYGKQDAT DKEVQQAIAE AHFEKDLHML PSGLETMVGE KGVALSGGQK
QRISIARALM ANPEILILDD SLSAVDAKTE AAIIKNIREN RKGKTTFILT HRLSAVEHAD
LILVMDGGVI AERGTHQELL ANNGWYREQY ERQQLFTAEE GGAGA
