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.
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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
//