ID LYTR_BACSU STANDARD; PRT; 306 AA. AC Q02115; DT 01-JUL-1993 (REL. 26, CREATED) DT 01-JUL-1993 (REL. 26, LAST SEQUENCE UPDATE) DT 01-JUL-1993 (REL. 26, LAST ANNOTATION UPDATE) DE MEMBRANE-BOUND PROTEIN LYTR. GN LYTR. OS BACILLUS SUBTILIS. OC PROKARYOTA; FIRMICUTES; ENDOSPORE-FORMING RODS AND COCCI; BACILLACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=168; RM 93018998 RA LAZAREVIC V., MARGOT P., SOLDO B., KARAMATA D.; RL J. GEN. MICROBIOL. 138:1949-1961(1992). CC -!- FUNCTION: ATTENUATOR ROLE FOR BOTH ITS OWN AND LYTABC OPERON CC EXPRESSION. CC -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN. TYPE II PROTEINS CC CONTAIN A N-TERMINAL MEMBRANE-ANCHORING DOMAIN WHICH IS NOT CC CLEAVED DURING BIOSYNTHESIS AND WHICH FUNCTION BOTH AS A CC TRANSLOCATION SIGNAL AND AS A MEMBRANE ANCHOR. 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; M87645; BSLYTABCD. KW MEMBRANE; SIGNAL-ANCHOR. FT DOMAIN 1 10 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 11 35 SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN). FT DOMAIN 35 306 EXTRACELLULAR (POTENTIAL). SQ SEQUENCE 306 AA; 34586 MW; 489486 CN; MRNERRKKKK TLLLTILTII GLLVLGTGGY AYYLWHKAAS TVASIHESID KSKKRDKEVS INKKDPFSVL IMGVDERDGD KGRADTLIYM TVNPKTNTTD MVSIPRDTYT KIIGKGTMDK INHSYAFGGT QMTVDTVENF LDVPVDYFVK VNMESFRDVV DTLGGITVNS TFAFSYDGYS FGKGEITLNG KEALAYTRMR KEDPRGDFGR QDRQRQVIQG IINKGANISS ITKFGDMFKV VENNVKTNLT FDNMWDIQSD YKGARKHIKQ HELKGTGTKI NGIYYYQADE SALSDITKEL KESLEK //