ID   OPPD_BACSU              Reviewed;         358 AA.
AC   P24136; P23365;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Oligopeptide transport ATP-binding protein OppD;
DE   AltName: Full=Stage 0 sporulation protein KD;
GN   Name=oppD; Synonyms=spo0KD; OrderedLocusNames=BSU11460;
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: Part of the binding protein-dependent transport system for
CC       oligopeptides. Probably responsible for energy coupling to the
CC       transport system. Required for sporulation and competence.
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}.
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DR   EMBL; X56347; CAA39790.1; -; Genomic_DNA.
DR   EMBL; M57689; AAA62691.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13003.1; -; Genomic_DNA.
DR   PIR; B69669; B69669.
DR   RefSeq; NP_389028.1; NC_000964.3.
DR   RefSeq; WP_010886477.1; NZ_CP053102.1.
DR   RefSeq; WP_014906294.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; P24136; -.
DR   SMR; P24136; -.
DR   STRING; 224308.BSU11460; -.
DR   PaxDb; P24136; -.
DR   PRIDE; P24136; -.
DR   EnsemblBacteria; CAB13003; CAB13003; BSU_11460.
DR   GeneID; 939814; -.
DR   KEGG; bsu:BSU11460; -.
DR   PATRIC; fig|224308.43.peg.1197; -.
DR   eggNOG; COG0444; Bacteria.
DR   InParanoid; P24136; -.
DR   OMA; YEPAHPY; -.
DR   PhylomeDB; P24136; -.
DR   BioCyc; BSUB:BSU11460-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
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   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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   TIGRFAMs; TIGR01727; oligo_HPY; 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..358
FT                   /note="Oligopeptide transport ATP-binding protein OppD"
FT                   /id="PRO_0000092653"
FT   DOMAIN          8..259
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         44..51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CONFLICT        337..358
FT                   /note="Missing (in Ref. 1; CAA39790)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        357
FT                   /note="V -> G (in Ref. 2; AAA62691)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   358 AA;  39764 MW;  8C387326BF348810 CRC64;
     MIRVTRLLEV KDLAISFKTY GGEVQAIRGV NFHLDKGETL AIVGESGSGK SVTSQAIMKL
     IPMPPGYFKR GEILFEGKDL VPLSEKEMQN VRGKEIGMIF QDPMTSLNPT MKVGKQITEV
     LFKHEKISKE AAKKRAVELL ELVGIPMPEK RVNQFPHEFS GGMRQRVVIA MALAANPKLL
     IADEPTTALD VTIQAQILEL MKDLQKKIDT SIIFITHDLG VVANVADRVA VMYAGQIVET
     GTVDEIFYDP RHPYTWGLLA SMPTLESSGE EELTAIPGTP PDLTNPPKGD AFALRSSYAM
     KIDFEQEPPM FKVSDTHYVK SWLLHPDAPK VEPPEAVKAK MRKLANTFEK PVLVREVE