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APPB_BACSU
ID   APPB_BACSU              Reviewed;         316 AA.
AC   P42062;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Oligopeptide transport system permease protein AppB;
GN   Name=appB; OrderedLocusNames=BSU11390;
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).
RN   [3]
RP   SEQUENCE REVISION TO 281-284.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
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; AAA62359.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12996.2; -; Genomic_DNA.
DR   PIR; I40546; I40546.
DR   RefSeq; NP_389021.2; NC_000964.3.
DR   RefSeq; WP_003245828.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; P42062; -.
DR   SMR; P42062; -.
DR   STRING; 224308.BSU11390; -.
DR   TCDB; 3.A.1.5.20; the atp-binding cassette (abc) superfamily.
DR   PRIDE; P42062; -.
DR   EnsemblBacteria; CAB12996; CAB12996; BSU_11390.
DR   GeneID; 936400; -.
DR   KEGG; bsu:BSU11390; -.
DR   PATRIC; fig|224308.179.peg.1225; -.
DR   eggNOG; COG0601; Bacteria.
DR   InParanoid; P42062; -.
DR   OMA; FADIPVM; -.
DR   PhylomeDB; P42062; -.
DR   BioCyc; BSUB:BSU11390-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; IPR045621; BPD_transp_1_N.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   Pfam; PF19300; BPD_transp_1_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..316
FT                   /note="Oligopeptide transport system permease protein AppB"
FT                   /id="PRO_0000059949"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        100..120
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        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        290..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          96..303
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   CONFLICT        281..284
FT                   /note="DYPV -> TIIRI (in Ref. 1; AAA62359)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   316 AA;  35278 MW;  90F879338D2B6253 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 DYPVIMAMTV ISAVLVVVGN
     LIADILYAIV DPRIEY
 
 
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