ID   REPB_STRAG              Reviewed;         210 AA.
AC   P13921;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Replication protein RepB;
GN   Name=repB;
OS   Streptococcus agalactiae.
OG   Plasmid pLS1, and Plasmid pMV158.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pLS1;
RX   PubMed=2438417; DOI=10.1016/0022-2836(86)90026-4;
RA   Lacks S.A., Lopez P., Greenberg B., Espinosa M.;
RT   "Identification and analysis of genes for tetracycline resistance and
RT   replication functions in the broad-host-range plasmid pLS1.";
RL   J. Mol. Biol. 192:753-765(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pMV158;
RX   PubMed=2677995; DOI=10.1093/nar/17.18.7283;
RA   van der Lelie D., Bron S., Venema G., Oskam L.;
RT   "Similarity of minus origins of replication and flanking open reading
RT   frames of plasmids pUB110, pTB913 and pMV158.";
RL   Nucleic Acids Res. 17:7283-7294(1989).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-36.
RC   PLASMID=pLS1;
RX   PubMed=2160544; DOI=10.1016/s0022-2836(05)80188-3;
RA   de la Campa A.G., del Solar G.H., Espinosa M.;
RT   "Initiation of replication of plasmid pLS1. The initiator protein RepB acts
RT   on two distant DNA regions.";
RL   J. Mol. Biol. 213:247-262(1990).
CC   -!- FUNCTION: Is essential for plasmid replication. Nicks the positive
CC       strand at the plus origin of replication.
CC   -!- INTERACTION:
CC       P13921; P13921: repB; NbExp=2; IntAct=EBI-7002529, EBI-7002529;
CC   -!- SIMILARITY: Belongs to the Gram-positive plasmids replication protein
CC       type 2 family. {ECO:0000305}.
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DR   EMBL; M29725; AAA98166.1; -; Genomic_DNA.
DR   EMBL; X15669; CAA33711.1; -; Genomic_DNA.
DR   PIR; B25599; B25599.
DR   PIR; S05981; S05981.
DR   RefSeq; NP_040421.1; NC_001380.1.
DR   RefSeq; WP_010889904.1; NC_010096.1.
DR   RefSeq; YP_001586272.1; NC_010096.1.
DR   PDB; 3DKX; X-ray; 2.70 A; A/B/C=1-210.
DR   PDB; 3DKY; X-ray; 3.60 A; A/B/C/D/E/F=1-210.
DR   PDB; 4U87; X-ray; 3.80 A; A/B/C=1-210.
DR   PDBsum; 3DKX; -.
DR   PDBsum; 3DKY; -.
DR   PDBsum; 4U87; -.
DR   AlphaFoldDB; P13921; -.
DR   SMR; P13921; -.
DR   MINT; P13921; -.
DR   EvolutionaryTrace; P13921; -.
DR   GO; GO:0005727; C:extrachromosomal circular DNA; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003916; F:DNA topoisomerase activity; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.1480; -; 1.
DR   InterPro; IPR002631; Plasmid_rep.
DR   InterPro; IPR041919; Plasmid_rep_C_sf.
DR   Pfam; PF01719; Rep_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; DNA replication; Plasmid.
FT   CHAIN           1..210
FT                   /note="Replication protein RepB"
FT                   /id="PRO_0000068331"
FT   CONFLICT        30
FT                   /note="G -> F (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          5..13
FT                   /evidence="ECO:0007829|PDB:3DKX"
FT   HELIX           15..17
FT                   /evidence="ECO:0007829|PDB:3DKX"
FT   HELIX           22..25
FT                   /evidence="ECO:0007829|PDB:3DKX"
FT   HELIX           26..29
FT                   /evidence="ECO:0007829|PDB:3DKX"
FT   STRAND          33..35
FT                   /evidence="ECO:0007829|PDB:3DKX"
FT   STRAND          48..51
FT                   /evidence="ECO:0007829|PDB:3DKX"
FT   STRAND          55..67
FT                   /evidence="ECO:0007829|PDB:3DKX"
FT   HELIX           68..79
FT                   /evidence="ECO:0007829|PDB:3DKX"
FT   HELIX           93..98
FT                   /evidence="ECO:0007829|PDB:3DKX"
FT   TURN            99..102
FT                   /evidence="ECO:0007829|PDB:3DKX"
FT   TURN            105..111
FT                   /evidence="ECO:0007829|PDB:3DKX"
FT   STRAND          121..123
FT                   /evidence="ECO:0007829|PDB:3DKX"
FT   HELIX           128..131
FT                   /evidence="ECO:0007829|PDB:3DKX"
FT   HELIX           136..152
FT                   /evidence="ECO:0007829|PDB:3DKX"
FT   HELIX           158..168
FT                   /evidence="ECO:0007829|PDB:3DKX"
FT   HELIX           169..172
FT                   /evidence="ECO:0007829|PDB:3DKX"
FT   HELIX           176..183
FT                   /evidence="ECO:0007829|PDB:3DKX"
FT   HELIX           187..201
FT                   /evidence="ECO:0007829|PDB:3DKX"
SQ   SEQUENCE   210 AA;  24250 MW;  E183126E7BA787FD CRC64;
     MAKEKARYFT FLLYPESIPS DWELKLETLG VPMAISPLHD KDKSSIKGQK YKKAHYHVLY
     IAKNPVTADS VRKKIKLLLG EKSLAMVQVV LNVENMYLYL THESKDAIAK KKHVYDKADI
     KLINNFDIDR YVTLDVEEKT ELFNVVVSLI RAYTLQNIFD LYDFIDENGE TYGLTINLVN
     EVIAGKTGFM KLLFDGAYQR SKRGTKNEER