ID   APPC_BACSU     STANDARD;      PRT;   303 AA.
AC   P42063;
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 appC.
GN   Name=appC; OrderedLocusNames=BSU11400;
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; AAA62360.1; -; Genomic_DNA.
DR   EMBL; Z99110; CAB12997.1; -; Genomic_DNA.
DR   PIR; I40547; I40547.
DR   SubtiList; BG11089; appC.
DR   GenomeReviews; AL009126_GR; BSU11400.
DR   BioCyc; BSUB1423:BSU1141-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    303       Oligopeptide transport system permease
FT                                protein appC.
FT                                /FTId=PRO_0000059950.
FT   TRANSMEM     39     59       Potential.
FT   TRANSMEM    103    123       Potential.
FT   TRANSMEM    138    158       Potential.
FT   TRANSMEM    165    183       Potential.
FT   TRANSMEM    212    232       Potential.
FT   TRANSMEM    269    289       Potential.
FT   DOMAIN       99    290       ABC transmembrane type-1.
SQ   SEQUENCE   303 AA;  33420 MW;  B9CD2CD936C46DC5 CRC64;
     MSELQTTPSP EIRLKENISK KPETMTKIFW EKFSKNKLAI LGAVILFIII MSAVFAPLIA
     PYPQEQQSLL DKYKAPGLEH LMGTDKFGRD IFSRILYGAR VSLLVGFASV VGSILIGTVL
     GALAGYFRGI VDAVIMRVVD IVLSIPDIFL LITLVTIFKP GVDKLILIFC LTGWTTTARL
     VRGEFLSLRS REYVLAAKTI GTKTHKIIFS HILPNALGPI IVSATLKVGS VILAESALSY
     LGFGIQPPIA SWGNMLQDAQ NFTVMIQAWW YPLFPGLFIL MTVLCFNFVG DGLRDALDPK
     NIK
//