ID   PRIB_ECOLI     STANDARD;      PRT;   103 AA.
AC   P07013;
DT   01-APR-1988 (REL. 07, CREATED)
DT   01-MAR-1992 (REL. 21, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   PRIMOSOMAL REPLICATION PROTEIN N.
GN   PRIB.
OS   ESCHERICHIA COLI.
OC   PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS;
OC   ENTEROBACTERIACEAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 86310297.
RA   SCHNIER J., KITAKAWA M., ISONO K.;
RL   MOL. GEN. GENET. 204:126-132(1986).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12 / MG1655;
RA   BURLAND V.D., PLUNKETT G. III, SOFIA H.J., DANIELS D.L.,
RA   BLATTNER F.R.;
RL   NUCLEIC ACIDS RES. 23:2105-2119(1995).
RN   [3]
RP   SEQUENCE OF 1-27, AND FUNCTION.
RC   STRAIN=K12;
RX   MEDLINE; 91310687.
RA   ZAVITZ K.H., DIGATE R.J., MARIANS K.J.;
RL   J. BIOL. CHEM. 266:13988-13995(1991).
RN   [4]
RP   SEQUENCE OF 1-27, AND FUNCTION.
RX   MEDLINE; 91268023.
RA   ALLEN G.C. JR., KORNBERG A.;
RL   J. BIOL. CHEM. 266:11610-11613(1991).
CC   -!- FUNCTION: PRIA RECOGNIZES A SPECIFIC HAIRPIN SEQUENCE ON PHIX
CC       SSDNA. THIS STRUCTURE IS THEN RECOGNIZED AND BOUND BY PROTEINS
CC       PRIB AND PRIC. FORMATION OF THE PRIMOSOME PROCEEDS WITH THE
CC       SUBSEQUENT ACTIONS OF DNAB, DNAC, DNAT AND PRIMASE.
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DR   EMBL; X04022; X04022.
DR   EMBL; U14003; U14003.
DR   PIR; A30281; Q4ECFR.
DR   ECOGENE; EG10764; PRIB.
KW   PRIMOSOME.
FT   INIT_MET      0      0
SQ   SEQUENCE   103 AA;  11311 MW;  53975 CN;
     TNRLVLSGTV CRAPLRKVSP SGIPHCQFVL EHRSVQEEAG FHRQAWCQMP VIVSGHENQA
     ITHSITVGSR ITVQGFISCH KAKNGLSKMV LHAEQIELID SGD
//