ID   MUKB_SALAR              Reviewed;        1488 AA.
AC   A9MHV9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=SARI_01968;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) 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; CP000880; ABX21849.1; -; Genomic_DNA.
DR   RefSeq; WP_000572755.1; NC_010067.1.
DR   AlphaFoldDB; A9MHV9; -.
DR   SMR; A9MHV9; -.
DR   STRING; 41514.SARI_01968; -.
DR   EnsemblBacteria; ABX21849; ABX21849; SARI_01968.
DR   KEGG; ses:SARI_01968; -.
DR   HOGENOM; CLU_004430_0_0_6; -.
DR   OMA; FIAVYQH; -.
DR   OrthoDB; 331846at2; -.
DR   Proteomes; UP000002084; 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..1488
FT                   /note="Chromosome partition protein MukB"
FT                   /id="PRO_1000088220"
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;  170020 MW;  1AE254A9AFE45026 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 VAEAAEMQEE NEARAEAAEL EVDELKSQLA DYQQALDVQQ TRAIQYNQAI
     SALARARELC HLPDLTPESA AEWLDTFQAK EQEATEKLLS LEQKMSVAQT AHSQFEQAYQ
     LVAAINGPLA RGEAWDVARE LLRDGVNQRH LAEQVQPLRM RLSELEQRLR EQQEAERLLA
     EFCKRQGKNF DIDELEALHQ ELEARIAALS DSVANASEQR LALRQEQEQL QSRIQHLMQR
     APVWLAAQNS LNQLSEQCGE AFSSSQEVTE YLQQLLERER EAIVERDEVG ARKNAVDEEI
     ERLSQPGGAE DQRLNTLAER FGGVLLSEIY DDVSLEDAPY FSALYGPSRH AIVVPDLSQI
     AEQLEGLTDC PEDLYLIEGD PQSFDDSVFS VDELEKAVVV KIADRQWRYS RFPSLPIFGR
     AARENRIESL HAEREVLSER FATLSFDVQK TQRLHQAFSR FIGSHLSVAF EDDPEAEIRR
     LNGRRVELER ALATHENDNQ QQRLQFEQAK EGVSALNRLL PRLNLLADET LADRVDEIQE
     RLDEAQEAAR FVQQYGNQLA KLEPVVSVLQ SDPEQFEQLK EDYAWSQQMQ RDARQQAFAL
     AEVVERRAHF SYSDSAEMLS GNSDLNEKLR QRLEQAEAER TRAREALRSH ASQLSQYSQV
     LASLKSSYDT KKELLNDLQR ELQDIGVRAD SGAEERARQR RDELHAQLSN NRSRRNQLEK
     ALTFCEAEMD 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