REPD_STAAU
ID REPD_STAAU Reviewed; 311 AA.
AC P03065;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Replication initiation protein;
GN Name=repD;
OS Staphylococcus aureus.
OG Plasmid pC221.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3860383; DOI=10.1002/j.1460-2075.1985.tb03665.x;
RA Brenner D.G., Shaw W.V.;
RT "The use of synthetic oligonucleotides with universal templates for rapid
RT DNA sequencing: results with staphylococcal replicon pC221.";
RL EMBO J. 4:561-568(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2993795; DOI=10.1007/bf00330758;
RA Projan S.J., Kornblum J., Moghazeh S.L., Edelman I., Gennaro M.L.,
RA Novick R.P.;
RT "Comparative sequence and functional analysis of pT181 and pC221, cognate
RT plasmid replicons from Staphylococcus aureus.";
RL Mol. Gen. Genet. 199:452-464(1985).
CC -!- FUNCTION: This protein is probably a specific topoisomerase involved in
CC initiating replication. This protein is specifically required and may
CC be rate-limiting for replication of the plasmid in vivo.
CC -!- MISCELLANEOUS: The nicking site of REP proteins is sequence, but not
CC plasmid, specific.
CC -!- SIMILARITY: Belongs to the plasmid replication initiation factor
CC family. {ECO:0000305}.
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DR EMBL; X02166; CAA26104.1; -; Genomic_DNA.
DR EMBL; X02529; CAA26366.1; -; Genomic_DNA.
DR PIR; A03601; RQSAD2.
DR RefSeq; NP_052693.1; NC_002129.1.
DR RefSeq; WP_002489526.1; NZ_NADF01000039.1.
DR RefSeq; YP_001595585.1; NC_010111.1.
DR RefSeq; YP_232726.1; NC_006977.1.
DR PDB; 4CWC; X-ray; 2.90 A; A/C=32-226.
DR PDB; 4CWE; X-ray; 3.00 A; A/C=32-226.
DR PDBsum; 4CWC; -.
DR PDBsum; 4CWE; -.
DR AlphaFoldDB; P03065; -.
DR SMR; P03065; -.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003916; F:DNA topoisomerase activity; IEA:InterPro.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR InterPro; IPR003491; Rep_trans.
DR Pfam; PF02486; Rep_trans; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA replication; Plasmid.
FT CHAIN 1..311
FT /note="Replication initiation protein"
FT /id="PRO_0000068323"
FT STRAND 39..50
FT /evidence="ECO:0007829|PDB:4CWC"
FT HELIX 53..65
FT /evidence="ECO:0007829|PDB:4CWC"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:4CWC"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:4CWC"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:4CWC"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:4CWC"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:4CWC"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:4CWC"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:4CWC"
FT HELIX 116..125
FT /evidence="ECO:0007829|PDB:4CWC"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:4CWC"
FT STRAND 131..146
FT /evidence="ECO:0007829|PDB:4CWC"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:4CWC"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:4CWC"
FT STRAND 169..177
FT /evidence="ECO:0007829|PDB:4CWC"
FT STRAND 179..189
FT /evidence="ECO:0007829|PDB:4CWC"
FT HELIX 190..196
FT /evidence="ECO:0007829|PDB:4CWC"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:4CWC"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:4CWC"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:4CWC"
SQ SEQUENCE 311 AA; 37479 MW; BE050FBD26387348 CRC64;
MSTENHSNYL QNKDLDNFSK TGYSNSRLSG NFFTTPQPEL SFDAMTIVGN LNKTNAKKLS
DFMSTEPQIR LWDILQTKFK AKALQEKVYI EYDKVKADSW DRRNMRVEFN PNKLTHEEML
WLKQNIIDYM EDDGFTRLDL AFDFEDDLSD YYAMTDKAVK KTIFYGRNGK PETKYFGVRD
SDRFIRIYNK KQERKDNADV EVMSEHLWRV EIELKRDMVD YWNDCFDDLH ILKPDWTTPE
KVKEQAMVYL LLNEEGTWGK LERHAKYKYK QLIKEISPID LTELMKSTLK ENEKQLQKQI
DFWQREFRFW K