ID   APPB_BACSU     STANDARD;      PRT;   317 AA.
AC   P42062;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   21-MAR-2006, entry version 42.
DE   Oligopeptide transport system permease protein appB.
GN   Name=appB; OrderedLocusNames=BSU11390;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=95089678; PubMed=7997159;
RA   Koide A., Hoch J.A.;
RT   "Identification of a second oligopeptide transport system in Bacillus
RT   subtilis and determination of its role in sporulation.";
RL   Mol. Microbiol. 13:417-426(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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).
CC   -!- FUNCTION: This protein is a component of an oligopeptide permease,
CC       a binding protein-dependent transport system. This APP system can
CC       completely substitute for the OPP system in both sporulation and
CC       genetic competence, though, unlike OPP, is incapable of
CC       transporting tripeptides. Probably responsible for the
CC       translocation of the substrate across the membrane (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Bacterial cell membrane; multi-pass membrane
CC       protein (Potential).
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport
CC       system permease family. OppBC subfamily.
CC   -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain.
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DR   EMBL; U20909; AAA62359.1; -; Genomic_DNA.
DR   EMBL; Z99110; CAB12996.1; -; Genomic_DNA.
DR   PIR; I40546; I40546.
DR   SubtiList; BG11088; appB.
DR   GenomeReviews; AL009126_GR; BSU11390.
DR   BioCyc; BSUB1423:BSU1140-MONOMER; -.
DR   InterPro; IPR000515; BPD_transp.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   PROSITE; PS50928; ABC_TM1; 1.
KW   Competence; Complete proteome; Membrane; Peptide transport;
KW   Protein transport; Sporulation; Transmembrane; Transport.
FT   CHAIN         1    317       Oligopeptide transport system permease
FT                                protein appB.
FT                                /FTId=PRO_0000059949.
FT   TRANSMEM     10     30       Potential.
FT   TRANSMEM    100    120       Potential.
FT   TRANSMEM    138    158       Potential.
FT   TRANSMEM    177    197       Potential.
FT   TRANSMEM    240    260       Potential.
FT   TRANSMEM    291    311       Potential.
FT   DOMAIN       96    304       ABC transmembrane type-1.
SQ   SEQUENCE   317 AA;  35400 MW;  D92ED0CF97088C96 CRC64;
     MAAYIIRRTL MSIPILLGIT ILSFVIMKAA PGDPMTLMMD PKISQADREQ FIEKYGLNDP
     QYVQYLKWLG NMVQGDFGTS IVRKGTPVSE LIMARLPNTL LLMLVSTILA LMISIPFGVL
     SAKRPYSKID YGITFTSFIG LAIPNFWFGL ILIMVLSVNL GWFPTGGVET LNTEFNIFDR
     IHHLILPAFV LATADMAGLT RYTRSNMLDV LNQDYIRTAR AKGFKENRVL FKHGLRNALL
     PVITIFGLMI PSFIGGSVVV EQIFTWPGLG KLFVDSAFQR TIIRIIMAMT VISAVLVVVG
     NLIADILYAI VDPRIEY
//