ID   MUKB_PECAS              Reviewed;        1479 AA.
AC   Q6D447;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Chromosome partition protein MukB {ECO:0000255|HAMAP-Rule:MF_01800};
DE   AltName: Full=Structural maintenance of chromosome-related protein {ECO:0000255|HAMAP-Rule:MF_01800};
GN   Name=mukB {ECO:0000255|HAMAP-Rule:MF_01800}; OrderedLocusNames=ECA2547;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
CC   -!- FUNCTION: Plays a central role in chromosome condensation, segregation
CC       and cell cycle progression. Functions as a homodimer, which is
CC       essential for chromosome partition. Involved in negative DNA
CC       supercoiling in vivo, and by this means organize and compact
CC       chromosomes. May achieve or facilitate chromosome segregation by
CC       condensation DNA from both sides of a centrally located replisome
CC       during cell division. {ECO:0000255|HAMAP-Rule:MF_01800}.
CC   -!- SUBUNIT: Homodimerization via its hinge domain. Binds to DNA via its C-
CC       terminal region. Interacts, and probably forms a ternary complex, with
CC       MukE and MukF via its C-terminal region. The complex formation is
CC       stimulated by calcium or magnesium. Interacts with tubulin-related
CC       protein FtsZ. {ECO:0000255|HAMAP-Rule:MF_01800}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000255|HAMAP-
CC       Rule:MF_01800}. Note=Restricted to the nucleoid region.
CC       {ECO:0000255|HAMAP-Rule:MF_01800}.
CC   -!- DOMAIN: The hinge domain, which separates the large intramolecular
CC       coiled coil regions, allows the homodimerization, forming a V-shaped
CC       homodimer. {ECO:0000255|HAMAP-Rule:MF_01800}.
CC   -!- SIMILARITY: Belongs to the SMC family. MukB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01800}.
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DR   EMBL; BX950851; CAG75446.1; -; Genomic_DNA.
DR   RefSeq; WP_011094092.1; NC_004547.2.
DR   AlphaFoldDB; Q6D447; -.
DR   SMR; Q6D447; -.
DR   STRING; 218491.ECA2547; -.
DR   EnsemblBacteria; CAG75446; CAG75446; ECA2547.
DR   KEGG; eca:ECA2547; -.
DR   PATRIC; fig|218491.5.peg.2580; -.
DR   eggNOG; COG3096; Bacteria.
DR   HOGENOM; CLU_004430_0_0_6; -.
DR   OMA; FIAVYQH; -.
DR   OrthoDB; 331846at2; -.
DR   Proteomes; UP000007966; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.70.3500; -; 1.
DR   HAMAP; MF_01800; MukB; 1.
DR   InterPro; IPR012090; MukB.
DR   InterPro; IPR032520; MukB_hinge.
DR   InterPro; IPR042501; MukB_hinge_sf.
DR   InterPro; IPR007406; MukB_N_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF04310; MukB; 1.
DR   Pfam; PF16330; MukB_hinge; 1.
DR   PIRSF; PIRSF005246; MukB; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Chromosome partition; Coiled coil;
KW   Cytoplasm; DNA condensation; DNA-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..1479
FT                   /note="Chromosome partition protein MukB"
FT                   /id="PRO_0000068217"
FT   REGION          666..783
FT                   /note="Flexible hinge"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          337..418
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          511..604
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          780..810
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          847..1116
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          1206..1265
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   BINDING         34..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
SQ   SEQUENCE   1479 AA;  169885 MW;  B560242155F70B50 CRC64;
     MIERGKFRSL TLVNWNGFFA RTFDLDELVT TLSGGNGAGK STTMAAFITA LIPDLTLLHF
     RNTTEAGATS GSRDKGLHGK LRAGVCYSTL DVVNSRHQRV LVGVRLQQVA GRDRKVDIKP
     FTIQGLPTAI QPTQILTQIV GDRQARVLSL QELKERVEEM EGVQFKQFNS ITDYHSLMFD
     LGVVPRRLRS ASDRSKFYRL IEASLYGGIS SAITRSLRDY LLPENSGVRK AFQDMEAALR
     ENRMTLEAIR VTQSDRDLFK HLISEATSYV AADYMRHANE RRIHLDGALE LRRDLFSSRK
     QLSSEQYRHV EMARELTEQN DTEGDLETDY QAASDHLNLV QTAMRQQEKI ERYNADLEEL
     SYRLEEQNEV VEEARDQQAE NEERADAAEL EVDELKSQLA DYQQALDVQQ TRAIQYQQAQ
     QALERARTLC QLPDLTAENA DEWLDSYQAR EQEATEILLM LEQKLSVADA AHGQFEQAYQ
     LVSKIAGAVS RSEAWQVARD LLRDSSSQRY QAERVQPLRM RLSELEQRLR EQQDAERLLQ
     DFSKRNGQDY QPEELESLQQ ELDARIETLS SLVAEAGERR MTLRQELEQT QQRIQKLTAR
     APVWLAAQET LTQLSEQSGE TFEDSRQVTE FMQQLLERER ETTVERDDIA ARKRQIEAQV
     DRLSQPGGSE DPRLNALAER FGGVLLSEIY DDVTLDDAPY FSALYGPSRH AIVVSDLSLI
     RDQLAGLEDC PEDLYLIEGD PQSFDDSVFA VDELERAVVV KVAERQWRYS RFPEVPLFGR
     AAREMRLEGL RDEREALAEQ YATLSFDVQK TQRLHQSFSR FIGTHLAVVF DEDPEAEIRT
     LSSRRGELDR AMASFDGENQ QQRQQYEQAK EASGQLNKLI PRISLLCDET LQDRVEEIRA
     ELDETEESAR FIQQHGVTLT KLEPLVSVLQ SDPQQHEQLQ EDYTQAQNAQ RQAKQQAFTL
     TEVVQRRAHF SYADSAGMLG ENAGLNDKLR HRLEQAEAER TKAREQLRQH QTQLTQYSQV
     QASLKSSYDA KQDMLKELLQ ELQDIGVRAD ADAEARARQR RDELHAALST NRSRRNQLEK
     QITFCEAEMD SVQKKLRKLE RDYHQMREQV VTAKAGWCTV MRLVKDNGVE RRLHRRELAY
     MEGDELRSMS DKALGALRLA VADNEHLRDV LRLSEDPKRP ERKIQFYIAV YQHLRERIRQ
     DIIRTDDPVE AIEQMEIELN RLTEELMARE QMLAISSRSV ANIIRKTIQR EQNRIRMLNQ
     GLQAVSFGQV KSVRLNVNVR ETHTTLLNVL SEQQEMHQDL FNSNRLTFSE ALAKLYQRLN
     PEIDMGQRTP QTIGEELLDY RNYLEMEVEV NRGADGWLRA ESGALSTGEA IGTGMSILVM
     VVQSWEEESK RLRGKDIIPC RLLFLDEAAR LDAKSIATLF ELCDRLEMQL VIAAPENISP
     EKGTTYKLVR KVYQNNEHVH VVGLRGFGTE TPETQEPAS