ID   MUKB_CROS8              Reviewed;        1482 AA.
AC   A7MEV9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=ESA_02418;
OS   Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-894;
RX   PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA   Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA   Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA   Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA   McClelland M., Forsythe S.J.;
RT   "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT   hybridization analysis with other Cronobacter species.";
RL   PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU77664.1; -; Genomic_DNA.
DR   RefSeq; WP_012125205.1; NC_009778.1.
DR   AlphaFoldDB; A7MEV9; -.
DR   SMR; A7MEV9; -.
DR   PRIDE; A7MEV9; -.
DR   EnsemblBacteria; ABU77664; ABU77664; ESA_02418.
DR   KEGG; esa:ESA_02418; -.
DR   PATRIC; fig|290339.8.peg.2148; -.
DR   HOGENOM; CLU_004430_0_0_6; -.
DR   OMA; FIAVYQH; -.
DR   OrthoDB; 331846at2; -.
DR   Proteomes; UP000000260; 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..1482
FT                   /note="Chromosome partition protein MukB"
FT                   /id="PRO_1000069907"
FT   REGION          666..783
FT                   /note="Flexible hinge"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   REGION          1049..1077
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          337..418
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          444..472
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          509..601
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          781..805
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          835..1116
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          1210..1265
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COMPBIAS        1049..1074
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   1482 AA;  168909 MW;  6F384E6407401BED CRC64;
     MIERGKFRSL TLINWNGFFA RTFDLDELVT TLSGGNGAGK STTMAAFVTA LIPDLTLLHF
     RNTTEAGATS GSRDKGLHGK LKAGVCYSVL DVVNSRHQRV LVGVRLQQVA GRDRKVDIKP
     FAIQGLPSAI LPTQLLTETL NDRQARVLSL NELKDKIDTM EGVQLKQFNS ITDYHSLMFD
     LGVVARRLRS ASDRSKYYRL IEASLYGGIS SAITRSLRDY LLPENGGVRK AFQDMEAALR
     ENRMTLEAIR VTQSDRDLFK HLISEATNYV AADYMRHANE RRIHLDQALE LRRELFSSRK
     QLAAEQYKHV HMARELSEHA GAEGDLETDY QAASDHLNLV QTALRQQEKI ERYEADLEEL
     QIRLEEQSEV VAEAAEQQEE NEARAEAAEL EVDELKSQLA DYQQALDVQQ TRAIQYQQAL
     TALERARELC HLPDLSADSA DEWLDTYQAK EQEATERLLS LEQKMSVAQT AHSQFEQAYQ
     LVASINGPVS RAEAWDVARE LLRDASQQRH LAEQVQPLRM RLSELEQRLR EQQDAERLLA
     EFCKRQGKNY DPEDLEALND ELEARIAALS DSVSQAGEQR MTLRQELEQI QSRVKTLTSH
     APAWLAAQNS LNQISEQSGE TFESGQQVTE YLQQLLERER EAIVERDEVG ARKRAVDEEI
     ERLSQPGGAE DARLNALAER FGGVLLSEIY DDVSFDDAPY FSALYGPSRH AIVVPDLSRV
     RDLLDGLEDC PEDLYLIEGD PQSFDDSVFS VEELEKAVVV KVAERQWRYS RFPSVPLFGR
     AARESRIESL HAEREALSER YATLSFDVQK TQRLHQAFSR FVGQHLAVAF EADPEAEIRK
     LNTRRSEIER AISQHENDNQ QQRVQFEQAK EGVAQLNRLL PRLSLLADDS LADRVEEIQE
     RLAEAQDAAR FLSQHGKALA KLEPVASVLQ SDPEQFDQLK QDYEQARQTQ RDARQQAFAL
     SEVVQRRAHF SYSDSAQMLN GNTDLNEKLR QRLEQAEAER TRAREALRTH AAKLSQYHQV
     LASLKSSFDT KKELLGDLQR ELQDIGVRAD AGAEERARQR RDELHTRLSN NRSRRNQLEK
     QLTLCEAEMD NLTRSLKRLE RNYHEMREQV VSAKAGWCAV MRMVKDNGVE RRLHRRELAY
     HSGDDLRSMS DKALGALRLA VADNEHLRDV LRLSEDPKRP ERKIQFFVAV YQHLRERIRQ
     DIIRTDDPVE AIEQMEIELG RLTEELTSRE QKLAISSRSV ANIIRKTIQR EQNRIRMLNQ
     GLQSVSFGQV NSVRLNVNVR ESHATLLEVL AEQHEQHQDL FNSNRLTFSE ALAKLWQRLN
     PQIDMGQRTA QTIGEELLDY RNYLEMEVEV NRGSDGWLRA ESGALSTGEA IGTGMSILVM
     VVQSWEDESS RLRGKDISPC RLLFLDEAAR LDARSIATLF ELCERLQMQL IIAAPENISP
     EKGTTYKLVR KVFQNHEHVH VVGLRGFAAP PADALPGPAE VS