ID OPPF_BACSU Reviewed; 305 AA. AC P24137; O31599; P23366; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 14-APR-2009, sequence version 3. DT 29-MAY-2024, entry version 157. DE RecName: Full=Oligopeptide transport ATP-binding protein OppF {ECO:0000305}; DE EC=7.4.2.6 {ECO:0000305|PubMed:1901616}; DE AltName: Full=Stage 0 sporulation protein KE; GN Name=oppF {ECO:0000303|PubMed:1901616}; GN Synonyms=spo0KE {ECO:0000303|PubMed:1899858}; OrderedLocusNames=BSU11470; OS Bacillus subtilis (strain 168). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=224308; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, AND DISRUPTION RP PHENOTYPE. RC STRAIN=168; RX PubMed=1901616; DOI=10.1111/j.1365-2958.1991.tb01838.x; 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 in the RT initiation of sporulation."; RL Mol. Microbiol. 5:173-185(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=168; RX PubMed=1899858; DOI=10.1128/jb.173.4.1388-1398.1991; RA Rudner D.Z., Ledeaux J.R., Ireton K., Grossman A.D.; RT "The spo0K locus of Bacillus subtilis is homologous to the oligopeptide RT permease locus and is required for sporulation and competence."; RL J. Bacteriol. 173:1388-1398(1991). RN [3] 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 [4] RP INDUCTION BY TNRA. RX PubMed=12823818; DOI=10.1046/j.1365-2958.2003.03567.x; RA Yoshida K., Yamaguchi H., Kinehara M., Ohki Y.-H., Nakaura Y., Fujita Y.; RT "Identification of additional TnrA-regulated genes of Bacillus subtilis RT associated with a TnrA box."; RL Mol. Microbiol. 49:157-165(2003). CC -!- FUNCTION: Part of the ABC transporter complex OppABCDF involved in the CC uptake of oligopeptides (PubMed:1901616). Probably responsible for CC energy coupling to the transport system (Probable). Required for CC genetic competence but not for peptide transport or for sporulation CC (PubMed:1899858, PubMed:1901616). {ECO:0000269|PubMed:1899858, CC ECO:0000269|PubMed:1901616, ECO:0000305}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a [peptide](out) + ATP + H2O = a [peptide](in) + ADP + H(+) + CC phosphate; Xref=Rhea:RHEA:78459, Rhea:RHEA-COMP:19083, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33710, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.4.2.6; CC Evidence={ECO:0000305|PubMed:1901616}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78460; CC Evidence={ECO:0000305|PubMed:1901616}; CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (OppD and CC OppF), two transmembrane proteins (OppB and OppC) and a solute-binding CC protein (OppA). {ECO:0000305|PubMed:1901616}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane CC protein {ECO:0000305}. CC -!- INDUCTION: Positively regulated by TnrA under nitrogen-limited CC conditions. {ECO:0000269|PubMed:12823818}. CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene does not affect the CC sporulation process but causes a defect in competence (PubMed:1899858, CC PubMed:1901616). Disruption does not affect resistance to bialaphos CC (PubMed:1901616). {ECO:0000269|PubMed:1899858, CC ECO:0000269|PubMed:1901616}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA62692.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAA39791.1; Type=Erroneous initiation; Evidence={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; X56347; CAA39791.1; ALT_INIT; Genomic_DNA. DR EMBL; M57689; AAA62692.1; ALT_INIT; Genomic_DNA. DR EMBL; M57689; AAA62693.1; -; Genomic_DNA. DR EMBL; AL009126; CAB13004.1; -; Genomic_DNA. DR PIR; E38447; E38447. DR RefSeq; NP_389029.1; NC_000964.3. DR RefSeq; WP_003245567.1; NZ_JNCM01000035.1. DR AlphaFoldDB; P24137; -. DR SMR; P24137; -. DR STRING; 224308.BSU11470; -. DR jPOST; P24137; -. DR PaxDb; 224308-BSU11470; -. DR EnsemblBacteria; CAB13004; CAB13004; BSU_11470. DR GeneID; 936410; -. DR KEGG; bsu:BSU11470; -. DR PATRIC; fig|224308.179.peg.1233; -. DR eggNOG; COG4608; Bacteria. DR InParanoid; P24137; -. DR OrthoDB; 9802264at2; -. DR PhylomeDB; P24137; -. DR BioCyc; BSUB:BSU11470-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 PANTHER; PTHR43776:SF14; METAL-STAPHYLOPINE IMPORT SYSTEM ATP-BINDING PROTEIN CNTF; 1. DR PANTHER; PTHR43776; TRANSPORT ATP-BINDING PROTEIN; 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 1: Evidence at protein level; KW ATP-binding; Cell membrane; Competence; Membrane; Nucleotide-binding; KW Peptide transport; Protein transport; Reference proteome; Sporulation; KW Translocase; Transport. FT CHAIN 1..305 FT /note="Oligopeptide transport ATP-binding protein OppF" FT /id="PRO_0000092661" FT DOMAIN 6..251 FT /note="ABC transporter" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT BINDING 42..49 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT CONFLICT 266..269 FT /note="VRQK -> CSE (in Ref. 1; CAA39791)" FT /evidence="ECO:0000305" SQ SEQUENCE 305 AA; 34748 MW; 4D22B5C7C1797407 CRC64; MTEKLLEIKH LKQHFVTPRG TVKAVDDLSF DIYKGETLGL VGESGCGKST TGRSIIRLYE ATDGEVLFNG ENVHGRKSRK KLLEFNRKMQ MIFQDPYASL NPRMTVADII AEGLDIHKLA KTKKERMQRV HELLETVGLN KEHANRYPHE FSGGQRQRIG IARALAVDPE FIIADEPISA LDVSIQAQVV NLMKELQKEK GLTYLFIAHD LSMVKYISDR IGVMYFGKLV ELAPADELYE NPLHPYTKSL LSAIPLPDPD YERNRVRQKY DPSVHQLKDG ETMEFREVKP GHFVMCTEAE FKAFS //