PRE_STRAG
ID PRE_STRAG Reviewed; 494 AA.
AC P13925;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Plasmid recombination enzyme;
DE AltName: Full=Mobilization protein;
GN Name=pre; Synonyms=mob;
OS Streptococcus agalactiae.
OG Plasmid pMV158.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1311;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2768188; DOI=10.1128/jb.171.9.4778-4784.1989;
RA Priebe S.D., Lacks S.A.;
RT "Region of the streptococcal plasmid pMV158 required for conjugative
RT mobilization.";
RL J. Bacteriol. 171:4778-4784(1989).
CC -!- FUNCTION: The interaction of the RSA site and the PRE protein may not
CC only serves a function in plasmid maintenance, but may also contributes
CC to the distribution of small antibiotic resistance plasmids among Gram-
CC positive bacteria.
CC -!- MISCELLANEOUS: Contains conserved positively charged amino acids
CC probably involved in the binding of the pre protein to the RSA site.
CC -!- SIMILARITY: Belongs to the plasmid mobilization pre family.
CC {ECO:0000305}.
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DR EMBL; X15669; CAA33713.1; -; Genomic_DNA.
DR EMBL; M28538; AAA25387.1; -; Genomic_DNA.
DR PIR; A33952; A33952.
DR PIR; S10134; S10134.
DR RefSeq; WP_012218462.1; NC_010096.1.
DR RefSeq; YP_001586274.1; NC_010096.1.
DR PDB; 4LVI; X-ray; 1.90 A; A=2-199.
DR PDB; 4LVJ; X-ray; 2.17 A; A=2-199.
DR PDB; 4LVK; X-ray; 2.37 A; A=2-199.
DR PDB; 4LVL; X-ray; 2.20 A; A=2-199.
DR PDB; 4LVM; X-ray; 3.10 A; A/C=2-199.
DR PDB; 5N2Q; X-ray; 2.00 A; A=2-198.
DR PDBsum; 4LVI; -.
DR PDBsum; 4LVJ; -.
DR PDBsum; 4LVK; -.
DR PDBsum; 4LVL; -.
DR PDBsum; 4LVM; -.
DR PDBsum; 5N2Q; -.
DR AlphaFoldDB; P13925; -.
DR SMR; P13925; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR InterPro; IPR001668; Mob_Pre.
DR Pfam; PF01076; Mob_Pre; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Plasmid.
FT CHAIN 1..494
FT /note="Plasmid recombination enzyme"
FT /id="PRO_0000068425"
FT BINDING 44
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000255"
FT BINDING 115
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000255"
FT CONFLICT 213
FT /note="P -> L (in Ref. 2; AAA25387)"
FT /evidence="ECO:0000305"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:4LVI"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:4LVI"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:4LVL"
FT HELIX 37..42
FT /evidence="ECO:0007829|PDB:4LVI"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:4LVK"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:4LVM"
FT HELIX 55..66
FT /evidence="ECO:0007829|PDB:4LVI"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:4LVI"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:4LVI"
FT HELIX 97..115
FT /evidence="ECO:0007829|PDB:4LVI"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:4LVI"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:4LVI"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:4LVI"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:4LVI"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:4LVI"
FT HELIX 154..170
FT /evidence="ECO:0007829|PDB:4LVI"
FT HELIX 189..194
FT /evidence="ECO:0007829|PDB:4LVI"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:4LVM"
SQ SEQUENCE 494 AA; 57859 MW; 91CB07E698AF6D99 CRC64;
MSYMVARMQK MKAGNLGGAF KHNERVFETH SNKDINPSRS HLNYELTDRD RSVSYEKQIK
DYVNENKVSN RAIRKDAVLC DEWIITSDKD FFEKLDEEQT RTFFETAKNY FAENYGESNI
AYASVHLDES TPHMHMGVVP FENGKLSSKA MFDREELKHI QEDLPRYMSD HGFELERGKL
NSEAKHKTVA EFKRAMADME LKEELLEKYH APPFVDERTG ELNNDTEAFW HEKEFADMFE
VQSPIRETTN QEKMDWLRKQ YQEELKKLES SKKPLEDDLS HLEELLDKKT KEYIKIDSEA
SERASELSKA EGYINTLENH SKSLEAKIEC LESDNLQLEK QKATKLEAKA LNESELRELK
PKKNFLGKEH YELSPEQFEG LKAEVYRSRT LLHHKDIELE QAKRQVSLRA SKNYFTASLE
RAKEKAKGES IDRLKSEIKR LKNENSILRQ QNDKMLGKLR ELMPDKAFKN LLSELKAIKP
IVNIIKKAIE KSLF