ID   APPF_BACSU              Reviewed;         329 AA.
AC   P42065;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Oligopeptide transport ATP-binding protein AppF;
GN   Name=appF; OrderedLocusNames=BSU11370;
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 197.
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 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}.
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; AAA62357.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12994.2; -; Genomic_DNA.
DR   PIR; I40544; I40544.
DR   RefSeq; NP_389019.2; NC_000964.3.
DR   RefSeq; WP_003232964.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; P42065; -.
DR   SMR; P42065; -.
DR   STRING; 224308.BSU11370; -.
DR   TCDB; 3.A.1.5.20; the atp-binding cassette (abc) superfamily.
DR   PaxDb; P42065; -.
DR   PRIDE; P42065; -.
DR   EnsemblBacteria; CAB12994; CAB12994; BSU_11370.
DR   GeneID; 936390; -.
DR   KEGG; bsu:BSU11370; -.
DR   PATRIC; fig|224308.179.peg.1222; -.
DR   eggNOG; COG4608; Bacteria.
DR   InParanoid; P42065; -.
DR   OMA; AFGPKVH; -.
DR   PhylomeDB; P42065; -.
DR   BioCyc; BSUB:BSU11370-MON; -.
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: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   Gene3D; 3.40.50.300; -; 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   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF08352; oligo_HPY; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01727; oligo_HPY; 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..329
FT                   /note="Oligopeptide transport ATP-binding protein AppF"
FT                   /id="PRO_0000091932"
FT   DOMAIN          10..261
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         53..60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CONFLICT        197
FT                   /note="A -> P (in Ref. 1; AAA62357)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   329 AA;  37086 MW;  2D2D4D27BFB043F6 CRC64;
     MTAANQETIL ELRDVKKYFP IRSGLFQRKV GDVKAVDGVS FSLKKGETLG IVGESGCGKS
     TAGRTMIRLY KPTEGQILFK GQDISNLSEE KLRKSVRKNI QMVFQDPFAS LNPRKTLRSI
     IKEPFNTHNM YTMRERNEKV EELLARVGLH PSFAGRYPHE FSGGQRQRIG IARALTLNPE
     LIIADEPVSA LDVSIQAQVI NLMEELQEEF NLTYLFISHD LSVVRHISDR VGVMYLGKMM
     ELTGKHELYD NPLHPYTQAL LSSVPVTRKR GSVKRERIVL KGELPSPANP PKGCVFHTRC
     PVAKPICKEQ IPEFKEAAPS HFVACHLYS