ID   APPD_BACSU              Reviewed;         328 AA.
AC   P42064;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=Oligopeptide transport ATP-binding protein AppD;
GN   Name=appD; OrderedLocusNames=BSU11360;
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).
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 energy coupling to the transport
CC       system.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; U20909; AAA62356.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12993.1; -; Genomic_DNA.
DR   PIR; I40543; I40543.
DR   RefSeq; NP_389018.1; NC_000964.3.
DR   RefSeq; WP_003232965.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; P42064; -.
DR   SMR; P42064; -.
DR   STRING; 224308.BSU11360; -.
DR   TCDB; 3.A.1.5.20; the atp-binding cassette (abc) superfamily.
DR   PaxDb; 224308-BSU11360; -.
DR   EnsemblBacteria; CAB12993; CAB12993; BSU_11360.
DR   GeneID; 936391; -.
DR   KEGG; bsu:BSU11360; -.
DR   PATRIC; fig|224308.179.peg.1221; -.
DR   eggNOG; COG0444; Bacteria.
DR   InParanoid; P42064; -.
DR   OrthoDB; 9802264at2; -.
DR   PhylomeDB; P42064; -.
DR   BioCyc; BSUB:BSU11360-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   CDD; cd03257; ABC_NikE_OppD_transporters; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR013563; Oligopep_ABC_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR01727; oligo_HPY; 1.
DR   PANTHER; PTHR43297; OLIGOPEPTIDE TRANSPORT ATP-BINDING PROTEIN APPD; 1.
DR   PANTHER; PTHR43297:SF2; OLIGOPEPTIDE TRANSPORT ATP-BINDING PROTEIN APPD; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF08352; oligo_HPY; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Competence; Membrane; Nucleotide-binding;
KW   Peptide transport; Protein transport; Reference proteome; Sporulation;
KW   Transport.
FT   CHAIN           1..328
FT                   /note="Oligopeptide transport ATP-binding protein AppD"
FT                   /id="PRO_0000091931"
FT   DOMAIN          5..256
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         41..48
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   328 AA;  36311 MW;  E4B87CD2B9D27F25 CRC64;
     MSTLLEVNNL KTYFFRKKEP IPAVDGVDFH ISKGETVALV GESGSGKSIT SLSIMGLVQS
     SGGKIMDGSI KLEDKDLTSF TENDYCKIRG NEVSMIFQEP MTSLNPVLTI GEQITEVLIY
     HKNMKKKEAR QRAVELLQMV GFSRAEQIMK EYPHRLSGGM RQRVMIAIAL SCNPKLLIAD
     EPTTALDVTI QAQVLELMKD LCQKFNTSIL LITHDLGVVS EAADRVIVMY CGQVVENATV
     DDLFLEPLHP YTEGLLTSIP VIDGEIDKLN AIKGSVPTPD NLPPGCRFAP RCPKAMDKCW
     TNQPSLLTHK SGRTVRCFLY EEEGAEQS
//