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DescriptionRecName: Full=Oligopeptide transport ATP-binding protein AppF;
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MyHits synonymsAPPF_BACSU , P42065 , 2D2D4D27BFB043F6
match map segment
iprf:ABC_TRANSPORTER_2 ipfam:ABC_tran ipfam:oligo_HPY ismart:AAA ipat:ABC_TRANSPORTER_1  
Legends: 1, CONFLICT A -> P (in Ref. 1; AAA62357). {ECO:0000305}; 2, NP_BIND ATP. {ECO:0000255|PROSITE- ProRule:PRU00434}; 3, ipat:ABC_TRANSPORTER_1 [T].
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   10-MAY-2017, entry version 121.
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.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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.,
RA   Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus
RT   subtilis 168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
CC   -!- FUNCTION: This protein is a component of an oligopeptide permease,
CC       a 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
CC       transporting tripeptides. Probably responsible for energy coupling
CC       to the transport system.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC       {ECO:0000305}.
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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   ProteinModelPortal; P42065; -.
DR   SMR; P42065; -.
DR   STRING; 224308.Bsubs1_010100006281; -.
DR   TCDB; 3.A.1.5.20; the atp-binding cassette (abc) superfamily.
DR   PaxDb; P42065; -.
DR   EnsemblBacteria; CAB12994; CAB12994; BSU11370.
DR   GeneID; 936390; -.
DR   KEGG; bsu:BSU11370; -.
DR   PATRIC; 18973986; VBIBacSub10457_1187.
DR   eggNOG; ENOG4108JQ7; Bacteria.
DR   eggNOG; COG4608; LUCA.
DR   InParanoid; P42065; -.
DR   KO; K02032; -.
DR   OMA; APVVHGM; -.
DR   PhylomeDB; P42065; -.
DR   BioCyc; BSUB:BSU11370-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:ATPase activity; IEA:InterPro.
DR   GO; GO:0030420; P:establishment of competence for transformation; 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   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_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; Complete proteome; Membrane;
KW   Nucleotide-binding; Peptide transport; Protein transport;
KW   Reference proteome; Sporulation; Transport.
FT   CHAIN         1    329       Oligopeptide transport ATP-binding
FT                                protein AppF.
FT                                /FTId=PRO_0000091932.
FT   DOMAIN       10    261       ABC transporter. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00434}.
FT   NP_BIND      53     60       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00434}.
FT   CONFLICT    197    197       A -> P (in Ref. 1; AAA62357).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        10    261       iprf:ABC_TRANSPORTER_2 [T]
FT   MYHIT        37    188       ipfam:ABC_tran [T]
FT   MYHIT       240    307       ipfam:oligo_HPY [T]
FT   MYHIT        45    238       ismart:AAA [T]
FT   MYHIT       161    175       ipat:ABC_TRANSPORTER_1 [T]
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
//