ID   YHEH_BACSU              Reviewed;         673 AA.
AC   O07549; Q796W5;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Probable multidrug resistance ABC transporter ATP-binding/permease protein YheH;
DE            EC=7.6.2.-;
GN   Name=yheH; OrderedLocusNames=BSU09720;
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; CAA74449.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12811.1; -; Genomic_DNA.
DR   PIR; H69828; H69828.
DR   RefSeq; NP_388853.1; NC_000964.3.
DR   RefSeq; WP_003233292.1; NZ_JNCM01000035.1.
DR   PDB; 7M33; EM; 3.55 A; D=1-673.
DR   PDBsum; 7M33; -.
DR   AlphaFoldDB; O07549; -.
DR   SMR; O07549; -.
DR   STRING; 224308.BSU09720; -.
DR   TCDB; 3.A.1.106.8; the atp-binding cassette (abc) superfamily.
DR   PaxDb; O07549; -.
DR   PRIDE; O07549; -.
DR   EnsemblBacteria; CAB12811; CAB12811; BSU_09720.
DR   GeneID; 939287; -.
DR   KEGG; bsu:BSU09720; -.
DR   PATRIC; fig|224308.179.peg.1045; -.
DR   eggNOG; COG1132; Bacteria.
DR   InParanoid; O07549; -.
DR   OMA; VMVPQDG; -.
DR   PhylomeDB; O07549; -.
DR   BioCyc; BSUB:BSU09720-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:0034040; F:ATPase-coupled lipid transmembrane transporter activity; IBA:GO_Central.
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..673
FT                   /note="Probable multidrug resistance ABC transporter ATP-
FT                   binding/permease protein YheH"
FT                   /id="PRO_0000376078"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        347..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          18..398
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          430..664
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         463..470
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   673 AA;  76305 MW;  533DDC9970E9B8D5 CRC64;
     MKIGKTLWRY ALLYRKLLIT AVLLLTVAVG AELTGPFIGK KMIDDHILGI EKTWYEAAEK
     DKNAVQFHGV SYVREDRLQE PVSKAKEAHI YQVGMAFYFV DQAVSFDGNR TVSDGKLTIT
     NGDKSRAYAA EKLTKQELFQ FYQPEIKGMV LLICLYGGLL VFSVFFQYGQ HYLLQMSANR
     IIQKMRQDVF SHIQKMPIRY FDNLPAGKVV ARITNDTEAI RDLYVTVLST FVTSGIYMFG
     IFTALFLLDV KLAFVCLAIV PIIWLWSVIY RRYASYYNQK IRSINSDINA KMNESIQGMT
     IIQAFRHQKE TMREFEELNE SHFYFQNRML NLNSLMSHNL VNVIRNLAFV CLIWHFGGAS
     LNAAGIVSIG VLYAFVDYLN RLFQPITGIV NQFSKLELAR VSAGRVFELL EEKNTEEAGE
     PAKERALGRV EFRDVSFAYQ EGEEVLKHIS FTAQKGETVA LVGHTGSGKS SILNLLFRFY
     DAQKGDVLID GKSIYNMSRQ ELRSHMGIVL QDPYLFSGTI GSNVSLDDER MTEEEIKNAL
     RQVGAEPLLK KLPKGINEPV IEKGSTLSSG ERQLISFARA LAFDPAILIL DEATAHIDTE
     TEAVIQKALD VVKQGRTTFV IAHRLSTIRN ADQILVLDKG EIVERGNHEE LMALEGQYYQ
     MYELQKGQKH SIA