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 02-NOV-2016, entry version 118.
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}.
CC -!- SIMILARITY: Contains 1 ABC transporter domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00434}.
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 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: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.
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 45 238 ismart:AAA [T]
FT MYHIT 240 307 ipfam:oligo_HPY [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
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