ID OPPF_BACSU Reviewed; 308 AA. AC P24137; O31599; P23366; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 05-FEB-2008, entry version 67. DE Oligopeptide transport ATP-binding protein oppF. GN Name=oppF; Synonyms=spo0KE; OrderedLocusNames=BSU11470; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=91194547; PubMed=1901616; RA Perego M., Higgins C.F., Pearce S.R., Gallagher M.P., Hoch J.A.; RT "The oligopeptide transport system of Bacillus subtilis plays a role RT in the initiation of sporulation."; RL Mol. Microbiol. 5:173-185(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=91139580; PubMed=1899858; RA Rudner D.Z., Ledeaux J.R., Ireton K., Grossman A.D.; RT "The spo0K locus of Bacillus subtilis is homologous to the RT oligopeptide permease locus and is required for sporulation and RT competence."; RL J. Bacteriol. 173:1388-1398(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=98044033; 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). CC -!- FUNCTION: Component of the oligopeptide permease, a binding CC protein-dependent transport system. Necessary for genetic CC competence but not sporulation. Probably responsible for energy CC coupling to the transport system. CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. CC -!- SIMILARITY: Belongs to the ABC transporter family. CC -!- SIMILARITY: Contains 1 ABC transporter domain. 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; X56347; CAA39791.1; -; Genomic_DNA. DR EMBL; M57689; AAA62692.1; -; Genomic_DNA. DR EMBL; M57689; AAA62693.1; ALT_INIT; Genomic_DNA. DR EMBL; Z99110; CAB13004.1; ALT_INIT; Genomic_DNA. DR PIR; E38447; E38447. DR RefSeq; NP_389029.1; -. DR HSSP; Q9YGA6; 1G29. DR GeneID; 936410; -. DR GenomeReviews; AL009126_GR; BSU11470. DR KEGG; bsu:BG10775; -. DR SubtiList; BG10775; oppF. DR BioCyc; BSUB224308:BSU1148-MON; -. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR003593; AAA+_ATPase_core. DR InterPro; IPR003439; ABC_transp_like. DR InterPro; IPR013563; Oligopep_ABC_C. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF08352; oligo_HPY; 1. DR ProDom; PD000006; ABC_transporter; 1. DR SMART; SM00382; AAA; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Competence; Complete proteome; Membrane; KW Nucleotide-binding; Peptide transport; Protein transport; Sporulation; KW Transport. FT CHAIN 1 308 Oligopeptide transport ATP-binding FT protein oppF. FT /FTId=PRO_0000092661. FT DOMAIN 9 254 ABC transporter. FT NP_BIND 45 52 ATP (Potential). FT CONFLICT 269 272 VRQK -> CSE (in Ref. 1). SQ SEQUENCE 308 AA; 35104 MW; F17DE0016AA3E4ED CRC64; MNELTEKLLE IKHLKQHFVT PRGTVKAVDD LSFDIYKGET LGLVGESGCG KSTTGRSIIR LYEATDGEVL FNGENVHGRK SRKKLLEFNR KMQMIFQDPY ASLNPRMTVA DIIAEGLDIH KLAKTKKERM QRVHELLETV GLNKEHANRY PHEFSGGQRQ RIGIARALAV DPEFIIADEP ISALDVSIQA QVVNLMKELQ KEKGLTYLFI AHDLSMVKYI SDRIGVMYFG KLVELAPADE LYENPLHPYT KSLLSAIPLP DPDYERNRVR QKYDPSVHQL KDGETMEFRE VKPGHFVMCT EAEFKAFS //