PRIC_ECOLI
ID PRIC_ECOLI Reviewed; 175 AA.
AC P23862; Q2MBW0;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Primosomal replication protein N'';
GN Name=priC; OrderedLocusNames=b0467, JW0456;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-19.
RC STRAIN=K12;
RX PubMed=1856227; DOI=10.1016/s0021-9258(18)92800-0;
RA Zavitz K.H., Digate R.J., Marians K.J.;
RT "The priB and priC replication proteins of Escherichia coli. Genes, DNA
RT sequence, overexpression, and purification.";
RL J. Biol. Chem. 266:13988-13995(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
CC -!- FUNCTION: PriA recognizes a specific hairpin sequence on bacteriophage
CC phi X174 ssDNA. This structure is then recognized and bound by proteins
CC PriB and PriC. Formation of the primosome proceeds with the subsequent
CC actions of DnaB, DnaC, DnaT and primase.
CC -!- INTERACTION:
CC P23862; P0ACJ8: crp; NbExp=2; IntAct=EBI-1117383, EBI-547513;
CC P23862; P0ACB0: dnaB; NbExp=5; IntAct=EBI-1117383, EBI-548978;
CC P23862; P77732: rhmR; NbExp=3; IntAct=EBI-1117383, EBI-549004;
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DR EMBL; D13958; BAA03055.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40221.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73569.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76246.1; -; Genomic_DNA.
DR PIR; JQ1149; JQ1149.
DR RefSeq; NP_415000.1; NC_000913.3.
DR RefSeq; WP_000844874.1; NZ_SSZK01000009.1.
DR PDB; 2RT6; NMR; -; A=1-98.
DR PDBsum; 2RT6; -.
DR AlphaFoldDB; P23862; -.
DR BMRB; P23862; -.
DR SMR; P23862; -.
DR BioGRID; 4262816; 50.
DR BioGRID; 849460; 13.
DR ComplexPortal; CPX-1952; Replication restart pre-primosome complex, priAC variant.
DR ComplexPortal; CPX-1953; Replication restart pre-primosome complex priC-rep variant.
DR ComplexPortal; CPX-5909; Replication restart primosome complex, priAC variant.
DR ComplexPortal; CPX-5911; Replication restart primosome complex, priC-rep variant.
DR DIP; DIP-10564N; -.
DR IntAct; P23862; 25.
DR STRING; 511145.b0467; -.
DR jPOST; P23862; -.
DR PaxDb; P23862; -.
DR PRIDE; P23862; -.
DR EnsemblBacteria; AAC73569; AAC73569; b0467.
DR EnsemblBacteria; BAE76246; BAE76246; BAE76246.
DR GeneID; 945071; -.
DR KEGG; ecj:JW0456; -.
DR KEGG; eco:b0467; -.
DR PATRIC; fig|1411691.4.peg.1809; -.
DR EchoBASE; EB0758; -.
DR eggNOG; COG3923; Bacteria.
DR HOGENOM; CLU_103284_0_0_6; -.
DR OMA; FDRQLFS; -.
DR PhylomeDB; P23862; -.
DR BioCyc; EcoCyc:EG10765-MON; -.
DR BioCyc; MetaCyc:EG10765-MON; -.
DR PRO; PR:P23862; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990159; C:DnaB-DnaC-DnaT-PriA-PriC complex; IC:ComplexPortal.
DR GO; GO:1990160; C:DnaB-DnaC-Rep-PriC complex; IC:ComplexPortal.
DR GO; GO:1990077; C:primosome complex; IC:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR GO; GO:0006270; P:DNA replication initiation; IDA:EcoCyc.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IC:ComplexPortal.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IC:ComplexPortal.
DR GO; GO:0006261; P:DNA-templated DNA replication; IMP:EcoCyc.
DR GO; GO:0031297; P:replication fork processing; IC:ComplexPortal.
DR Gene3D; 1.20.1270.340; -; 1.
DR InterPro; IPR038338; PriB/PriC_sf.
DR InterPro; IPR010890; Primosomal_replicat_PriB/PriC.
DR Pfam; PF07445; PriC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Primosome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1856227"
FT CHAIN 2..175
FT /note="Primosomal replication protein N''"
FT /id="PRO_0000058574"
FT HELIX 3..20
FT /evidence="ECO:0007829|PDB:2RT6"
FT TURN 23..27
FT /evidence="ECO:0007829|PDB:2RT6"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:2RT6"
FT HELIX 46..63
FT /evidence="ECO:0007829|PDB:2RT6"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:2RT6"
FT HELIX 69..93
FT /evidence="ECO:0007829|PDB:2RT6"
SQ SEQUENCE 175 AA; 20375 MW; 6C735A9CAABB82B3 CRC64;
MKTALLLEKL EGQLATLRQR CAPVSQFATL SARFDRHLFQ TRATTLQACL DEAGDNLAAL
RHAVEQQQLP QVAWLAEHLA AQLEAIAREA SAWSLREWDS APPKIARWQR KRIQHQDFER
RLREMVAERR ARLARVTDLV EQQTLHREVE AYEARLARCR HALEKIENRL ARLTR
