ID OPPF_BACSU STANDARD; PRT; 308 AA. AC P24137; P23366; O31599; DT 01-MAR-1992 (Rel. 21, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 01-OCT-2000 (Rel. 40, Last annotation update) DE OLIGOPEPTIDE TRANSPORT ATP-BINDING PROTEIN OPPF. GN OPPF OR SPO0KE. OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillus/Clostridium group; OC Bacillus/Staphylococcus group; Bacillus. OX NCBI_TaxID=1423; RN [1] RP SEQUENCE FROM N.A. 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 SEQUENCE FROM N.A. 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 SEQUENCE FROM N.A. RC STRAIN=168; RA Kunst F., Ogasawara N., Yoshikawa H., Danchin A.; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. 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: MEMBRANE-ASSOCIATED. CC -!- SIMILARITY: BELONGS TO THE ATP-BINDING TRANSPORT PROTEIN FAMILY CC (ABC TRANSPORTERS). OPPD AND OPPF SHOW AN EXTENSIVE HOMOLOGY WITH CC EACH OTHER. 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; -. DR EMBL; M57689; AAA62692.1; -. DR EMBL; M57689; AAA62693.1; ALT_INIT. DR EMBL; Z99110; CAB13004.1; ALT_INIT. DR PIR; S15234; S15234. DR PIR; E38447; E38447. DR SubtiList; BG10775; oppF. DR InterPro; IPR003593; AAA. DR InterPro; IPR003439; ABC_transportr. DR InterPro; IPR001687; ATP_GTP_A. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR PROSITE; PS00211; ABC_TRANSPORTER; 1. KW Peptide transport; Transport; Membrane; ATP-binding; Sporulation. FT NP_BIND 45 52 ATP (BY SIMILARITY). 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 //