PRE3_STAAC
ID PRE3_STAAC Reviewed; 413 AA.
AC Q5HJZ6;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Plasmid recombination enzyme type 3;
DE AltName: Full=Mobilization protein;
DE AltName: Full=Plasmid recombinase;
GN Name=pre; OrderedLocusNames=SAA0003;
OS Staphylococcus aureus (strain COL).
OG Plasmid pT181.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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. {ECO:0000250}.
CC -!- MISCELLANEOUS: Contains conserved positively charged amino acids
CC probably involved in the binding of the pre protein to the RSA site.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the plasmid mobilization pre family.
CC {ECO:0000305}.
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DR EMBL; CP000045; AAW36314.1; -; Genomic_DNA.
DR RefSeq; WP_000122374.1; NC_006629.2.
DR AlphaFoldDB; Q5HJZ6; -.
DR SMR; Q5HJZ6; -.
DR EnsemblBacteria; AAW36314; AAW36314; SAA0003.
DR GeneID; 50019750; -.
DR GeneID; 61682014; -.
DR GeneID; 66909090; -.
DR KEGG; sac:SAA0003; -.
DR HOGENOM; CLU_035698_0_0_9; -.
DR OMA; VEDYFER; -.
DR Proteomes; UP000000530; Plasmid pT181.
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 3: Inferred from homology;
KW DNA-binding; Plasmid.
FT CHAIN 1..413
FT /note="Plasmid recombination enzyme type 3"
FT /id="PRO_0000224927"
FT REGION 179..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 45
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"
SQ SEQUENCE 413 AA; 48526 MW; 8F16FF8D82998659 CRC64;
MSYSIVRVSK VKSGTNTTGI QKHVQRENNN YENEDIDHSK TYLNYDLVNA NKQNFNNLID
EKIEQNYTGK RKIRTDAIKH IDGLITSDND FFDNQTPEDT KQFFEYAKEF LEQEYGKDNL
LYATVHMDEK TPHMHYGVVP ITDDGRLSAK EVVGNKKALT AFQDRFNEHV KQRGYDLERG
QSRQVTNAKH EQISQYKQKT EYHKQEYERE SQKTDHIKQK NDKLMQEYQK SLNTLKKPIN
VPYEQETEKV GGLFSKEIQE TGNVVISQKD FNEFQKQIKA AQDISEDYEY IKSGRALDDK
DKEIREKDDL LNKAVERIEN ADDNFNQLYE NAKPLKENIE IALKLLKILL KELERVLGRN
TFAERVNKLT EDEPKLNGLA GNLDKKMNPE LYSEQEQQQE QQKNQKRDRG MHL