ID   APPC_BACSU              Reviewed;         303 AA.
AC   P42063;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Oligopeptide transport system permease protein AppC;
GN   Name=appC; OrderedLocusNames=BSU11400;
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=7997159; DOI=10.1111/j.1365-2958.1994.tb00436.x;
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   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).
CC   -!- FUNCTION: This protein is a component of an oligopeptide permease, a
CC       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 transporting
CC       tripeptides. Probably responsible for the translocation of the
CC       substrate across the membrane (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. OppBC subfamily. {ECO:0000305}.
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DR   EMBL; U20909; AAA62360.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12997.1; -; Genomic_DNA.
DR   PIR; I40547; I40547.
DR   RefSeq; NP_389022.1; NC_000964.3.
DR   RefSeq; WP_003232961.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; P42063; -.
DR   IntAct; P42063; 1.
DR   STRING; 224308.BSU11400; -.
DR   TCDB; 3.A.1.5.20; the atp-binding cassette (abc) superfamily.
DR   PaxDb; P42063; -.
DR   PRIDE; P42063; -.
DR   EnsemblBacteria; CAB12997; CAB12997; BSU_11400.
DR   GeneID; 936394; -.
DR   KEGG; bsu:BSU11400; -.
DR   PATRIC; fig|224308.179.peg.1226; -.
DR   eggNOG; COG1173; Bacteria.
DR   InParanoid; P42063; -.
DR   OMA; RAWWVVS; -.
DR   PhylomeDB; P42063; -.
DR   BioCyc; BSUB:BSU11400-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:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR   GO; GO:0015833; P:peptide transport; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   CDD; cd06261; TM_PBP2; 1.
DR   Gene3D; 1.10.3720.10; -; 1.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   InterPro; IPR025966; OppC_N.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   Pfam; PF12911; OppC_N; 1.
DR   SUPFAM; SSF161098; SSF161098; 1.
DR   PROSITE; PS50928; ABC_TM1; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Competence; Membrane; Peptide transport; Protein transport;
KW   Reference proteome; Sporulation; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..303
FT                   /note="Oligopeptide transport system permease protein AppC"
FT                   /id="PRO_0000059950"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        165..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          99..290
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
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