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 27-MAR-2024, entry version 132.
DE RecName: Full=Oligopeptide transport system permease protein AppB;
GN Name=appB; OrderedLocusNames=BSU11390;
OS Bacillus subtilis (strain 168).
OC Bacteria; Bacillota; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 PaxDb; 224308-BSU11390; -.
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 OrthoDB; 9773683at2; -.
DR PhylomeDB; P42062; -.
DR BioCyc; BSUB:BSU11390-MONOMER; -.
DR Proteomes; UP000001570; Chromosome.
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; MetI-like; 1.
DR InterPro; IPR045621; BPD_transp_1_N.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR PANTHER; PTHR43163; DIPEPTIDE TRANSPORT SYSTEM PERMEASE PROTEIN DPPB-RELATED; 1.
DR PANTHER; PTHR43163:SF6; DIPEPTIDE TRANSPORT SYSTEM PERMEASE PROTEIN DPPB-RELATED; 1.
DR Pfam; PF00528; BPD_transp_1; 1.
DR Pfam; PF19300; BPD_transp_1_N; 1.
DR SUPFAM; SSF161098; MetI-like; 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
//
