ID   MUKB_CITK8              Reviewed;        1489 AA.
AC   A8AIF5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=CKO_02144;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-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; CP000822; ABV13268.1; -; Genomic_DNA.
DR   RefSeq; WP_012133000.1; NC_009792.1.
DR   AlphaFoldDB; A8AIF5; -.
DR   SMR; A8AIF5; -.
DR   STRING; 290338.CKO_02144; -.
DR   PRIDE; A8AIF5; -.
DR   EnsemblBacteria; ABV13268; ABV13268; CKO_02144.
DR   GeneID; 45136085; -.
DR   KEGG; cko:CKO_02144; -.
DR   HOGENOM; CLU_004430_0_0_6; -.
DR   OMA; FIAVYQH; -.
DR   OrthoDB; 331846at2; -.
DR   Proteomes; UP000008148; 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..1489
FT                   /note="Chromosome partition protein MukB"
FT                   /id="PRO_1000069900"
FT   REGION          666..783
FT                   /note="Flexible hinge"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
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          780..805
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          835..919
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          977..1116
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          1209..1266
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   1489 AA;  170073 MW;  729312523037BEA8 CRC64;
     MIERGKFRSL TLINWNGFFA RTFDLDELVT TLSGGNGAGK STTMAAFVTA LIPDLTLLHF
     RNTTEAGATS GSRDKGLHGK LKAGVCYSML DVLNSRHQRV VVGVRLQQVA GRDRKVDIKP
     FAIQGLPMSV QPTQLVTETL NERQARVLTL AELKEKLDAM EGVQFKQFNS ITDYHSLMFD
     LGIIARRLRS ASDRSKFYRL IEASLYGGIS SAITRSLRDY LLPENSGVRK AFQDMEAALR
     ENRMTLEAIR VTQSDRDLFK HLISEATNYV AADYMRHANE RRVHLDKALE FRRELYTSRK
     QLAAEQYKHV DMARELGEHN GAEGDLEADY QAASDHLNLV QTALRQQEKI ERYEADLDEL
     QIRLEEQNEV VAEAADMQEE NEARAEAAEL EVDELKSQLA DYQQALDVQQ TRAIQYNQAI
     QALDRAKALC HLPDLTADSA AEWLETFQAK EQEATEKLLS LEQKMSVAQT AHSQFEQAYQ
     LVAAINGPLA RNEAWSVARD LLREGVEQRH LAEQVQPLRM RLSELEQRLR EQQEAERLLA
     EFCKRQGKHF DIDELEALHQ ELEARIAALS DSVSNAHEQR MTLRQEQEQL QSRIQHLMQR
     APIWLAAQNS LNQLCEQSGE EFTSSQDVTE YLQQLLERER EAIVERDEVG ARKNAVDEEI
     ERLSQPGGSE DSRLNALAER FGGVLLSEIY DDVSFEDAPY FSALYGPSRH AIVVPDLSLI
     AEQLEGLTDC PEDLYFIEGD PQSFDDSVFS VDELENAVVV KTAERQWRYS RFPTVPIFGR
     AARENRIESL HAEREGLSER FATLSFDVQK TQRLHQAFSR FIGSHLAVAF EADPEAEIRQ
     LNGRRVELER ALATHENDNQ QQRIQFEQAK EGVSALNRLL PRLNLLADDT LADRVDEIQE
     RLDDAQEAAR FIQQHGNQLA KLEPIVSVLQ NDPEQFEQLK EDYAYSQQTQ RDARQQAFAL
     TEVVQRRAHF SYSDSAEMLS GNSDLNEKLR QRLEQAEAER TRAREALRGH AAQLSQYNQV
     LASLKSSYDT KKELLGDLQR ELQDIGVRAD SGSEERARIR RDELHTQLSN NRSRRNQLEK
     ALTFCEAEMD NLTRRLRKLE RDYHEMREQV VTAKAGWCAV MRMVKDNGVE RRLHRRELAY
     LSADELRSMS DKALGALRLA VADNEHLRDV LRMSEDPKRP ERKIQFFVAV YQHLRERIRQ
     DIIRTDDPVE AIEQMEIELS RLTEELTSRE QKLAISSRSV ANIIRKTIQR EQNRIRMLNQ
     GLQNVSFGQV NSVRLNVNVR ETHATLLDVL SEQHEQHQDL FNSNRLTFSE ALAKLYQRLN
     PQIDMGQRTP QTIGEELLDY RNYLEMEVEV NRGSDGWLRA ESGALSTGEA IGTGMSILVM
     VVQSWEDEGR RLRGKDISPC RLLFLDEAAR LDARSIATLF ELCERLQMQL IIAAPENISP
     EKGTTYKLVR KVFHNTEHVH VVGLRGFAPQ LSETLPGTGT EDASSQAAG