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   03-AUG-2022, entry version 149.
DE   RecName: Full=Oligopeptide transport ATP-binding protein OppF;
DE   AltName: Full=Stage 0 sporulation protein KE;
GN   Name=oppF; Synonyms=spo0KE; OrderedLocusNames=BSU11470;
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=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].
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: Component of the oligopeptide permease, a binding protein-
CC       dependent transport system. Necessary for genetic competence but not
CC       sporulation. Probably responsible for energy coupling to the transport
CC       system.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC   -!- INDUCTION: Positively regulated by TnrA under nitrogen-limited
CC       conditions. {ECO:0000269|PubMed:12823818}.
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};
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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; P24137; -.
DR   PRIDE; P24137; -.
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   OMA; VFYKGQD; -.
DR   PhylomeDB; P24137; -.
DR   BioCyc; BSUB:BSU11470-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   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell membrane; Competence; Membrane; Nucleotide-binding;
KW   Peptide transport; Protein transport; Reference proteome; Sporulation;
KW   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