PARB4_ECOLX
ID PARB4_ECOLX Reviewed; 281 AA.
AC P22997; Q52337; Q56389;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Protein ParB;
GN Name=parB;
OS Escherichia coli.
OG Plasmid IncP-alpha RP4.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2172207; DOI=10.1128/jb.172.11.6194-6203.1990;
RA Gerlitz M., Hrabak O., Schwab H.;
RT "Partitioning of broad-host-range plasmid RP4 is a complex system involving
RT site-specific recombination.";
RL J. Bacteriol. 172:6194-6203(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 105-190.
RX PubMed=8387603; DOI=10.1006/jmbi.1993.1228;
RA Kholodii G.Y., Yurieva O.V., Lomovskaya O.L., Gorlenko Z.M., Mindlin S.Z.,
RA Nikiforov V.G.;
RT "Tn5053, a mercury resistance transposon with integron's ends.";
RL J. Mol. Biol. 230:1103-1107(1993).
CC -!- FUNCTION: Involved in plasmid partition.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA26416.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L40585; AAA98320.1; -; Genomic_DNA.
DR EMBL; M59825; AAA26415.1; -; Genomic_DNA.
DR EMBL; M59825; AAA26416.1; ALT_INIT; Genomic_DNA.
DR EMBL; L03728; AAA91496.1; -; Genomic_DNA.
DR PIR; C37141; C37141.
DR PIR; S32828; S32828.
DR AlphaFoldDB; P22997; -.
DR SMR; P22997; -.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0030541; P:plasmid partitioning; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.90; -; 1.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
DR InterPro; IPR002071; Thermonucl_AS.
DR Pfam; PF00565; SNase; 1.
DR SMART; SM00318; SNc; 1.
DR SUPFAM; SSF50199; SSF50199; 1.
DR PROSITE; PS01123; TNASE_1; 1.
DR PROSITE; PS01284; TNASE_2; 1.
DR PROSITE; PS50830; TNASE_3; 1.
PE 4: Predicted;
KW Endonuclease; Hydrolase; Nuclease; Plasmid; Plasmid partition.
FT CHAIN 1..281
FT /note="Protein ParB"
FT /id="PRO_0000215282"
FT DOMAIN 130..261
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..54
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 157
FT /evidence="ECO:0000250"
FT ACT_SITE 165
FT /evidence="ECO:0000250"
FT ACT_SITE 199
FT /evidence="ECO:0000250"
SQ SEQUENCE 281 AA; 31289 MW; 01907DD37F531370 CRC64;
MPARLGPNGY TQFDQGGRDE GGQALPTTSI HRLQHRGAGL RAWTRRHTRP AHPRPGARGP
RPARPGRVPF AGVRLAGGAG RLLQGQFRCS AAPGVPRSSA MGPRMKRRSY AMLRAAAALA
VLVVASPAWA ELRGEVVRII DGDTIDVLVD KQPVRVRLVD IDAPEKRQAF GERARQALAG
MVFRRHVLVD EKDTDRYGRT LGTVWVNMEL ASRPPQPRNV NAAMVHQGMA WAYRFHGRAA
DPEMLRLEQE ARGKRVGLWS DPHAVEPWKW RRESNNRRDE G