ID OPPF_BACSU STANDARD; PRT; 307 AA. AC P24137; P23366; DT 01-MAR-1992 (REL. 21, CREATED) DT 01-MAR-1992 (REL. 21, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE OLIGOPEPTIDE TRANSPORT ATP-BINDING PROTEIN OPPF. GN OPPF OR SPO0KE. OS BACILLUS SUBTILIS. OC BACTERIA; FIRMICUTES; BACILLUS/CLOSTRIDIUM GROUP; BACILLACEAE; OC BACILLUS. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=168; RX MEDLINE; 91194547. 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. 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). CC -!- FUNCTION: THIS PROTEIN IS A COMPONENT OF THE OLIGOPEPTIDE CC PERMEASE, A BINDING PROTEIN-DEPENDENT TRANSPORT SYSTEM. OPPF IS CC IS NECESSARY FOR GENETIC COMPETENCE BUT NOT SPORULATION, AND MAY CC BE RESPONSIBLE FOR ENERGY COUPLING TO THE TRANSPORT SYSTEM. CC -!- SUBCELLULAR LOCATION: MEMBRANE-ASSOCIATED. CC -!- SIMILARITY: BELONGS TO THE ATP-BINDING TRANSPORT PROTEIN FAMILY CC (ABC TRANSPORTERS). CC -!- SIMILARITY: OPPD AND OPPF SHOW AN EXTENSIVE HOMOLOGY WITH EACH CC OTHER. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; G580899; -. DR EMBL; M57689; G143608; -. DR EMBL; M57689; G551727; ALT_INIT. DR PIR; S15234; S15234. DR PIR; E38447; E38447. DR SUBTILIST; BG10775; OPPF. DR PROSITE; PS00211; ABC_TRANSPORTER; 1. DR PFAM; PF00005; ABC_tran; 1. KW PEPTIDE TRANSPORT; TRANSPORT; MEMBRANE; ATP-BINDING; SPORULATION. FT NP_BIND 45 52 ATP (BY SIMILARITY). FT CONFLICT 269 271 CSE -> VRQK (IN REF. 2). SQ SEQUENCE 307 AA; 34912 MW; 17715185 CRC32; 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 DPDYERNRCS EYDPSVHQLK DGETMEFREV KPGHFVMCTE AEFKAFS //