ID   MUKB_SALEP              Reviewed;        1488 AA.
AC   B5QZC8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=SEN0898;
OS   Salmonella enteritidis PT4 (strain P125109).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P125109;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(2008).
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; AM933172; CAR32481.1; -; Genomic_DNA.
DR   RefSeq; WP_000572746.1; NC_011294.1.
DR   AlphaFoldDB; B5QZC8; -.
DR   SMR; B5QZC8; -.
DR   KEGG; set:SEN0898; -.
DR   HOGENOM; CLU_004430_0_0_6; -.
DR   OMA; FIAVYQH; -.
DR   Proteomes; UP000000613; 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.
FT   CHAIN           1..1488
FT                   /note="Chromosome partition protein MukB"
FT                   /id="PRO_1000187483"
FT   REGION          666..783
FT                   /note="Flexible hinge"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   REGION          1049..1074
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          326..418
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          444..472
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          509..602
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          835..923
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          977..1116
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          1209..1265
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COMPBIAS        1049..1069
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         34..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
SQ   SEQUENCE   1488 AA;  170058 MW;  2E6D5280B7A90BAD CRC64;
     MIERGKFRSL TLINWNGFFA RTFDLDELVT TLSGGNGAGK STTMAAFVTA LIPDLTLLHF
     RNTTEAGATS GSRDKGLHGK LKAGVCYSML DTINSRHQRV VVGVRLQQVA GRDRKVDIKP
     FAIQGLPMSV QPTQLVTETL NERQARVLSL AELKDKLDEM EGVQFKQFNS ITDYHSLMFD
     LGIIARRLRS ASDRSKFYRL IEASLYGGIS SAITRSLRDY LLPENSGVRK AFQDMEAALR
     ENRLTLEAIR VTQSDRDLFK HLISEATDYV AADYMRHANE RRVHLDQALA FRRELYTSRK
     QLAAEQYKHV DMARELGEHN GAEGSLEADY QAASDHLNLV QTALRQQEKI ERYEADLEEL
     QIRLEEQNEV VAEAAEMQDE NEARAEAAEL EVDELKSQLA DYQQALDVQQ TRAIQYNQAI
     SALARAKELC HLPDLTPESA AEWLDTFQAK EQEATEKLLS LEQKMSVAQT AHSQFEQAYQ
     LVAAINGPLA RSEAWDVARE LLRDGVNQRH LAEQVQPLRM RLSELEQRLR EQQEAERLLA
     EFCKRQGKNF DIDELEALHQ ELEARIASLS ESVSSASEQR MALRQEQEQL QSRIQHLMQR
     APVWLAAQNS LNQLSEQCGE EFTSSQEVTE YLQQLLERER EAIVERDEVG ARKNAVDEEI
     ERLSQPGGAE DQRLNALAER FGGVLLSEIY DDVSLEDAPY FSALYGPSRH AIVVPDLSQI
     AEQLEGLTDC PEDLYLIEGD PQSFDDSVFS VDELEKAVVV KIADRQWRYS RFPSLPIFGR
     AARENRIESL HAEREVLSER FATLSFDVQK TQRLHQAFSR FIGSHLSVAF EDDPEAEIRR
     LNGRRVELER ALATHESDNQ QQRLQFEQAK EGVSALNRLL PRLNLLADET LADRVDEIQE
     RLDEAQEAAR FVQQYGNQLA KLEPVVSVLQ SDPEQFEQLK EDYAWSQQMQ RDARQQAFAL
     AEVVERRAHF SYSDSAEMLS GNSDLNEKLR QRLEQAEAER TRAREALRSH AAQLSQYSQV
     LASLKSSYDT KKELLNDLQR ELQDIGVRAD SGAEERARQR RDELHAQLSN NRSRRNQLEK
     ALTFCEAEME NLTRKLRKLE RDYHEMREQV VTAKAGWCAV MRMVKDNGVE RRLHRRELAY
     LSADELRSMS DKALGALRLA VADNEHLRDV LRLSEDPKRP ERKIQFFVAV YQHLRERIRQ
     DIIRTDDPVE AIEQMEIELS RLTEELTSRE QKLAISSRSV ANIIRKTIQR EQNRIRMLNQ
     GLQSVSFGQV NSVRLNVNVR ETHATLLDVL SEQQEQHQDL FNSNRLTFSE ALAKLYQRLN
     PQIDMGQRTP QTIGEELLDY RNYLEMEVEV NRGSDGWLRA ESGALSTGEA IGTGMSILVM
     VVQSWEDEAR RLRGKDISPC RLLFLDEAAR LDARSIATLF ELCERLQMQL IIAAPENISP
     EKGTTYKLVR KVFQNTEHVH VVGLRGFAPQ LPETLPGTQT EDTPSEAS