PIR_ECOLX
ID PIR_ECOLX Reviewed; 305 AA.
AC P03067; P10029;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=PI protein;
DE AltName: Full=Replication initiation protein;
GN Name=pir;
OS Escherichia coli.
OG Plasmid R6K.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3277861; DOI=10.1016/0014-5793(88)80573-8;
RA Inuzuka M., Wada Y.;
RT "An initiator protein for plasmid R6K DNA replication. Mutations affecting
RT the copy-number control.";
RL FEBS Lett. 228:7-11(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6291046; DOI=10.1073/pnas.79.18.5475;
RA Germino J., Bastia D.;
RT "Primary structure of the replication initiation protein of plasmid R6K.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:5475-5479(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3000771; DOI=10.1002/j.1460-2075.1985.tb03930.x;
RA Inuzuka M., Wada Y.;
RT "A single amino acid alteration in the initiation protein is responsible
RT for the DNA overproduction phenotype of copy number mutants of plasmid
RT R6K.";
RL EMBO J. 4:2301-2307(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RX PubMed=3857600; DOI=10.1073/pnas.82.9.2574;
RA Kelley W., Bastia D.;
RT "Replication initiator protein of plasmid R6K autoregulates its own
RT synthesis at the transcriptional step.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:2574-2578(1985).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 75-117.
RX PubMed=2277631; DOI=10.1007/bf00259447;
RA Greener A., Filutowicz M.S., McEachern M.J., Helinski D.R.;
RT "N-terminal truncated forms of the bifunctional pi initiation protein
RT express negative activity on plasmid R6K replication.";
RL Mol. Gen. Genet. 224:24-32(1990).
CC -!- FUNCTION: Initiation for plasmid R6K DNA replication.
CC -!- SUBUNIT: Homodimer.
CC -!- MISCELLANEOUS: The expression of PI protein is autoregulated.
CC -!- MISCELLANEOUS: PI protein binds to direct repeated sequences within
CC ori-gamma region for replication.
CC -!- SIMILARITY: Belongs to the initiator RepB protein family.
CC {ECO:0000305}.
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; Y00768; CAA68737.1; -; Genomic_DNA.
DR EMBL; J01779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M11128; AAA26084.1; -; Genomic_DNA.
DR PIR; S02261; IDECRK.
DR PDB; 2NRA; X-ray; 3.10 A; C=1-276.
DR PDBsum; 2NRA; -.
DR AlphaFoldDB; P03067; -.
DR SMR; P03067; -.
DR EvolutionaryTrace; P03067; -.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 2.
DR InterPro; IPR000525; Initiator_Rep_prot.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF01051; Rep_3; 1.
DR SUPFAM; SSF46785; SSF46785; 2.
PE 1: Evidence at protein level;
KW 3D-structure; DNA replication; Plasmid.
FT CHAIN 1..305
FT /note="PI protein"
FT /id="PRO_0000068415"
FT VARIANT 108
FT /note="T -> I (in mutant COP41)"
FT VARIANT 113
FT /note="P -> S (in mutant COP50)"
FT VARIANT 138
FT /note="T -> I (in mutants TS22 and TRCOP21)"
FT VARIANT 162
FT /note="A -> S (in mutants COP21 and TRCOP21)"
FT CONFLICT 128
FT /note="P -> N (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="F -> L (in Ref. 3)"
FT /evidence="ECO:0000305"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:2NRA"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:2NRA"
FT HELIX 22..27
FT /evidence="ECO:0007829|PDB:2NRA"
FT HELIX 30..41
FT /evidence="ECO:0007829|PDB:2NRA"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:2NRA"
FT HELIX 59..66
FT /evidence="ECO:0007829|PDB:2NRA"
FT HELIX 70..86
FT /evidence="ECO:0007829|PDB:2NRA"
FT HELIX 95..102
FT /evidence="ECO:0007829|PDB:2NRA"
FT STRAND 119..127
FT /evidence="ECO:0007829|PDB:2NRA"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:2NRA"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:2NRA"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:2NRA"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:2NRA"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:2NRA"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:2NRA"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:2NRA"
FT HELIX 169..180
FT /evidence="ECO:0007829|PDB:2NRA"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:2NRA"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:2NRA"
FT HELIX 195..202
FT /evidence="ECO:0007829|PDB:2NRA"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:2NRA"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:2NRA"
FT HELIX 220..226
FT /evidence="ECO:0007829|PDB:2NRA"
FT HELIX 228..238
FT /evidence="ECO:0007829|PDB:2NRA"
FT STRAND 239..250
FT /evidence="ECO:0007829|PDB:2NRA"
FT STRAND 258..265
FT /evidence="ECO:0007829|PDB:2NRA"
SQ SEQUENCE 305 AA; 34994 MW; 9E463E3E2AEDAEA2 CRC64;
MRLKVMMDVN KKTKIRHRNE LNHTLAQLPL PAKRVMYMAL APIDSKEPLE RGRVFKIRAE
DLAALAKITP SLAYRQLKEG GKLLGASKIS LRGDDIIALA KELNLPFTAK NSPEELDLNI
IEWIAYSPDE GYLSLKFTRT IEPYISSLIG KKNKFTTQLL TASLRLSSQY SSSLYQLIRK
HYSNFKKKNY FIISVDELKE ELIAYTFDKD GNIEYKYPDF PIFKRDVLNK AIAEIKKKTE
ISFVGFTVHE KEGRKISKLK FEFVVDEDEF SGDKDDEAFF MNLSEADAAF LKVFDETVPP
KKAKG