PARM_ECOLX
ID PARM_ECOLX Reviewed; 320 AA.
AC P11904; P10028;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Plasmid segregation protein ParM;
DE AltName: Full=ParA locus 36 kDa protein;
DE AltName: Full=Protein StbA;
GN Name=parM; Synonyms=stbA;
OS Escherichia coli.
OG Plasmid IncFII R100 (NR1), and Plasmid IncFII R1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KP245; PLASMID=IncFII R100 (NR1);
RX PubMed=3172224; DOI=10.1016/0022-2836(88)90282-3;
RA Tabuchi A., Min Y.-N., Kim C.K., Fan Y.-L., Womble D.D., Rownd R.H.;
RT "Genetic organization and nucleotide sequence of the stability locus of
RT IncFII plasmid NR1.";
RL J. Mol. Biol. 202:511-525(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=IncFII R1;
RX PubMed=3023637; DOI=10.1016/0022-2836(86)90001-x;
RA Gerdes K., Molin S.;
RT "Partitioning of plasmid R1. Structural and functional analysis of the parA
RT locus.";
RL J. Mol. Biol. 190:269-279(1986).
RN [3]
RP SEQUENCE REVISION TO 39 AND 60.
RA Gerdes K.;
RL Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=12486014; DOI=10.1093/emboj/cdf672;
RA van den Ent F., Moller-Jensen J., Amos L.A., Gerdes K., Lowe J.;
RT "F-actin-like filaments formed by plasmid segregation protein ParM.";
RL EMBO J. 21:6935-6943(2002).
CC -!- FUNCTION: Involved in the control of plasmid partition. Required for
CC the accurate segregation of the plasmid.
CC -!- SUBUNIT: Homopolymerizes into double helical protofilaments with a
CC longitudinal repeat similar to filamentous actin.
CC -!- INTERACTION:
CC P11904; P11904: parM; NbExp=5; IntAct=EBI-15658818, EBI-15658818;
CC -!- SIMILARITY: Belongs to the plasmid partition ParM family.
CC {ECO:0000305}.
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DR EMBL; X12777; CAA31264.1; -; Genomic_DNA.
DR EMBL; X04268; CAA27818.1; -; Genomic_DNA.
DR PIR; A24920; A24920.
DR RefSeq; NP_957570.1; NC_005327.1.
DR RefSeq; WP_000959884.1; NZ_WVVU01000024.1.
DR RefSeq; YP_001096425.1; NC_009133.1.
DR RefSeq; YP_002456142.1; NC_011812.1.
DR RefSeq; YP_003108258.1; NC_013121.1.
DR RefSeq; YP_006953486.1; NC_019073.1.
DR RefSeq; YP_006953911.1; NC_019090.1.
DR RefSeq; YP_006954241.1; NC_019095.1.
DR RefSeq; YP_006990723.1; NC_019424.1.
DR RefSeq; YP_007447518.1; NC_020278.2.
DR RefSeq; YP_008531404.1; NC_022333.1.
DR RefSeq; YP_009068579.1; NC_025141.1.
DR PDB; 1MWK; X-ray; 2.30 A; A/B=1-320.
DR PDB; 1MWM; X-ray; 2.00 A; A/B=1-320.
DR PDB; 2QU4; EM; 16.00 A; A=1-320.
DR PDB; 2ZGY; X-ray; 1.90 A; A/B=1-320.
DR PDB; 2ZGZ; X-ray; 2.25 A; A/B=1-320.
DR PDB; 2ZHC; EM; 23.80 A; A=1-320.
DR PDB; 3IKU; EM; -; A/B/C/D/E/F/G/H/I/J/K/L=1-320.
DR PDB; 3IKY; EM; -; A/B/C/D/E/F/G/H/I/J/K/L=1-320.
DR PDB; 4A61; X-ray; 2.00 A; A=2-320.
DR PDB; 4A62; X-ray; 2.20 A; A/B=1-320.
DR PDB; 4A6J; EM; 7.20 A; A/B/C/D/E/F/G/H/I/J=1-320.
DR PDB; 5AEY; EM; 4.30 A; A/B/C/D/E=1-318.
DR PDB; 5AI7; EM; -; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-318.
DR PDBsum; 1MWK; -.
DR PDBsum; 1MWM; -.
DR PDBsum; 2QU4; -.
DR PDBsum; 2ZGY; -.
DR PDBsum; 2ZGZ; -.
DR PDBsum; 2ZHC; -.
DR PDBsum; 3IKU; -.
DR PDBsum; 3IKY; -.
DR PDBsum; 4A61; -.
DR PDBsum; 4A62; -.
DR PDBsum; 4A6J; -.
DR PDBsum; 5AEY; -.
DR PDBsum; 5AI7; -.
DR AlphaFoldDB; P11904; -.
DR SMR; P11904; -.
DR DIP; DIP-29623N; -.
DR EvolutionaryTrace; P11904; -.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030541; P:plasmid partitioning; IEA:UniProtKB-KW.
DR CDD; cd10227; ParM_like; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR042051; ParM-like.
DR InterPro; IPR009440; Plasmid_segregation_ParM/StbA.
DR Pfam; PF06406; StbA; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Plasmid; Plasmid partition.
FT CHAIN 1..320
FT /note="Plasmid segregation protein ParM"
FT /id="PRO_0000068441"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2ZGY"
FT STRAND 9..17
FT /evidence="ECO:0007829|PDB:2ZGY"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:2ZGY"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:2ZGY"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:2ZGY"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:2ZGY"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:2ZGY"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:2ZGY"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:2ZGY"
FT HELIX 76..89
FT /evidence="ECO:0007829|PDB:2ZGY"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:2ZGY"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:2ZGY"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:2ZGY"
FT HELIX 116..125
FT /evidence="ECO:0007829|PDB:2ZGY"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:2ZGY"
FT STRAND 139..149
FT /evidence="ECO:0007829|PDB:2ZGY"
FT HELIX 150..159
FT /evidence="ECO:0007829|PDB:2ZGY"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:2ZGY"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:2ZGY"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:2ZGY"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:2ZGY"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:2ZGY"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:2ZGY"
FT HELIX 219..227
FT /evidence="ECO:0007829|PDB:2ZGY"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:2ZGY"
FT HELIX 232..238
FT /evidence="ECO:0007829|PDB:2ZGY"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:2ZGY"
FT HELIX 245..267
FT /evidence="ECO:0007829|PDB:2ZGY"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:2ZGY"
FT HELIX 283..292
FT /evidence="ECO:0007829|PDB:2ZGY"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:2ZGY"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:2ZGY"
FT HELIX 310..319
FT /evidence="ECO:0007829|PDB:2ZGY"
SQ SEQUENCE 320 AA; 35765 MW; 52B3239C0A567312 CRC64;
MLVFIDDGST NIKLQWQESD GTIKQHISPN SFKREWAVSF GDKKVFNYTL NGEQYSFDPI
SPDAVVTTNI AWQYSDVNVV AVHHALLTSG LPVSEVDIVC TLPLTEYYDR NNQPNTENIE
RKKANFRKKI TLNGGDTFTI KDVKVMPESI PAGYEVLQEL DELDSLLIID LGGTTLDISQ
VMGKLSGISK IYGDSSLGVS LVTSAVKDAL SLARTKGSSY LADDIIIHRK DNNYLKQRIN
DENKISIVTE AMNEALRKLE QRVLNTLNEF SGYTHVMVIG GGAELICDAV KKHTQIRDER
FFKTNNSQYD LVNGMYLIGN
