ID   MUKB_PECCP              Reviewed;        1479 AA.
AC   C6DFB1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=PC1_1779;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001657; ACT12820.1; -; Genomic_DNA.
DR   RefSeq; WP_015840027.1; NC_012917.1.
DR   AlphaFoldDB; C6DFB1; -.
DR   SMR; C6DFB1; -.
DR   STRING; 561230.PC1_1779; -.
DR   PRIDE; C6DFB1; -.
DR   EnsemblBacteria; ACT12820; ACT12820; PC1_1779.
DR   KEGG; pct:PC1_1779; -.
DR   eggNOG; COG3096; Bacteria.
DR   HOGENOM; CLU_004430_0_0_6; -.
DR   OMA; FIAVYQH; -.
DR   OrthoDB; 331846at2; -.
DR   Proteomes; UP000002736; 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; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Chromosome partition; Coiled coil;
KW   Cytoplasm; DNA condensation; DNA-binding; Nucleotide-binding.
FT   CHAIN           1..1479
FT                   /note="Chromosome partition protein MukB"
FT                   /id="PRO_1000215937"
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..603
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;  169667 MW;  D2737643B22E3B6D CRC64;
     MIERGKFRSL TLVNWNGFFA RTFDLDELVT TLSGGNGAGK STTMAAFITA LIPDLTLLHF
     RNTTEAGATS GSRDKGLHGK LRAGVCYSTL DVVNSRHQRV LVGVRLQQVA GRDRKVDIKP
     FTIQGLPTAI QPTQILTQVV GDRQARVLSL QELKDRVEEM EGVQFKQFNS ITDYHSLMFD
     LGVVPRRLRS ASDRSKFYRL IEASLYGGIS SAITRSLRDY LLPENSGVRK AFQDMEAALR
     ENRMTLEAIR VTQSDRDLFK HLISEATSYV AADYMRHANE RRIHLDGALE LRRDLFSSRK
     QLSSEQYRHV EMARELAEQS GAEGDLETDY QAASDHLNLV QTAMRQQEKI ERYNADLEEL
     SYRLEEQNEV VEEAREQQAE NEERADAAEL EVDELKSQLA DYQQALDVQQ TRAIQYQQAQ
     QALERARTLC QLPDLTADNA DEWLDSYQAK EQEATEILLM LEQKLSVADA AHGQFEQAYQ
     LVSKIAGAVN RNEAWQVARD LLRDSSSQRY QAERVQPLRM RLSELEQRLR EQQDAERLLQ
     DFSKRNGQDY QPEELESLQQ ELDARIETLS SLVAEAGERR MALRQELEQI QLRIQKLTTR
     APVWLAAQEM LTQLSEQSGE TFEDSRQVTE FMQQLLERER ETTVERDDIA SRKRQIEAQI
     ERLSQPGGSE DPRLNALAER FGGVLLSEIY DDVTLDDAPY FSALYGPSRH AIVVADLSLV
     REQLAGLEDC PEDLYLIEGD PQSFDDSVFA VEELERAVVV KVAERQWRYS RFPEVPLFGR
     AAREMRLESL RDEREALAEQ YATLSFDVQK TQRLHQSFSR FIGTHLAVVF DEDPEAEIRT
     LSSRRGELDR AIASFDGENQ QQRQQYEQAK EASVQLNKLI PRISLLCDET LQDRVEEIRA
     ELDETEESAR FIQQHGATLV KLEPLVSVLQ SDPQQHEQLQ EDYAQAQNAQ RQAKQQAFAL
     TEVVQRRAHF SYADSAGMLG ENAGLNDKLR HRLELAEAER TKAREQLRQH QAQLTQYSQV
     QASLKSSYDA KQDMLKELTQ ELQDIGVRAD ADAEERARQR RDELHAALST NRSRRNQLEK
     QITFCEAEMD SLQKKLRKLE RDYHQMREQV VTAKAGWCAV MRLVKDNGVE RRLHRRELAY
     MEGDELRSMS DKALGALRLA VADNEHLRDV LRLSEDPKRP ERKIQFYIAV YQHLRERIRQ
     DIIRTDDPVE AIEQMEIELN RLTEELTARE QMLAISSRSV ANIIRKTIQR EQNRIRMLNQ
     GLQAVAFGQV KSVRLNVNVR ETHTTLLNVL SEQQEMHQDL FNSNRLTFSE ALAKLYQRLN
     PEIDMGQRTP QTIGEELLDY RNYLEMEVEV NRGADGWLRA ESGALSTGEA IGTGMSILVM
     VVQSWEEESK RLRGKDIIPC RLLFLDEAAR LDAKSIATLF ELCDRLEMQL VIAAPENISP
     EKGTTYKLVR KVYQNNEHVH VVGLRGFGAE APDTQEQAS