ID   MUKB_HAEIN              Reviewed;        1510 AA.
AC   P45187;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 126.
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=HI_1374;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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; L42023; AAC23022.1; -; Genomic_DNA.
DR   PIR; D64120; D64120.
DR   RefSeq; NP_439526.1; NC_000907.1.
DR   RefSeq; WP_005693982.1; NC_000907.1.
DR   AlphaFoldDB; P45187; -.
DR   SMR; P45187; -.
DR   STRING; 71421.HI_1374; -.
DR   PRIDE; P45187; -.
DR   EnsemblBacteria; AAC23022; AAC23022; HI_1374.
DR   KEGG; hin:HI_1374; -.
DR   PATRIC; fig|71421.8.peg.1429; -.
DR   eggNOG; COG3096; Bacteria.
DR   HOGENOM; CLU_004430_0_0_6; -.
DR   OMA; FIAVYQH; -.
DR   PhylomeDB; P45187; -.
DR   BioCyc; HINF71421:G1GJ1-1400-MON; -.
DR   Proteomes; UP000000579; 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..1510
FT                   /note="Chromosome partition protein MukB"
FT                   /id="PRO_0000068220"
FT   REGION          707..824
FT                   /note="Flexible hinge"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          346..706
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          825..1154
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          1248..1304
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   BINDING         75..82
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
SQ   SEQUENCE   1510 AA;  173286 MW;  173EEC4198E3184F CRC64;
     MSDVFELENE IELESDEVIL ENENVEEIVD APIPFSMTTN NGIERGKFRS LTLINWNGFF
     ARTFDLDELV TTLSGGNGAG KSTTMAGFVT ALIPDLTLLH FRNTTEAGST GGSRDKGLHG
     KLRPGVCYAV LDTINSRHQR ILVGVRLQQI AGRDKKVDLK TFSIQGVELS QNPTALFTET
     VGEHQARVLN LNELKDKIEN IGAQFKQYHS ITDYHGMMFD LGIIPKRLRS ASDRSKFYKL
     IEASLYGGIS SAITRSLRDY LLPENLGVRK AFQDMESALR ENRMTLEAIK VTQSDRDLFK
     HLITETTNYV ASDYMRNANE RRGNIEAALE SRREWYKAKA EQNLSQHRLV DLSREVAELA
     ESERTLEVDH QSAVDHLNLV LNALRHQEKI TRYQEDIAEL TERLEEQKMV VEDANDALEE
     SQAQFEQTEI EIDAVRSQLA DYQQALDAQQ TRALQYQQAI AALEKAKTLC GLADLSVKNV
     EDYHAEFDAH AESLTETVLE LEHKMSISEA AKSQFDKAYQ LVCKIAGEMP RSTAWESAKE
     LLREYPSQKL QAQQTPQLRT KLHELEQRYA QQQSAVKLLN DFNQRANLSL QTAEELEDYH
     AEQEALIEDI SARLSEQVEN RSTLRQKREN LTALYDENAR KAPAWLTAQA ALERLEQQSG
     ERFEHSQDVM NFMQSQLVKE RELTMQRDQL EQKRLHLDEQ ISRLSQPDGS EDPRLNMLAE
     RFGGVLLSEL YDDVTIEDAP YFSALYGPSR HAIVVRDLNA VREQLAQLED CPDDLYLIEG
     DPTAFDDSVL SAQELELGVV VQVSDRELRY SRFPEIPLFG CAAREKRLEE LQIERDEVAE
     QHAQIAFDVQ KCQRLHEHFS QFVGLHLALA FQPNPEALMS EINRERNEID RELNQFNSGE
     QQLRIQLDNA KERLQLLNKL IPQLNVLADE DLIDRIEECR EQLDIAEQDE YFIRQHGVTL
     SQLEPIANSL QSDPENYEGL KNELTQAIER QKQVQQRVFA LADVVQRKPH FGYEDAGQAE
     TSELNEKLRQ RLEQMQAQRD TQREQVRQKQ SQFAEYNRVL IQLQSSYDSK YQLLNELIGE
     ISDLGVRADD GAEERARIRR DELHQQLSTS RQRRSYVEKQ LTLIESEADN LNRLIRKTER
     DYKTQRELVV AAKVSWCVVL RLSRNSDMEK RLNRRELAYL SADELRSMSD KALGALRTAV
     ADNEYLRDSL RVSEDSRKPE NKVRFFIAVY QHLRERIRQD IIKTDDPIDA IEQMEIELSR
     LTAELTGREK KLAISSESVA NIMRKTIQRE QNRIRMLNQG LQNIAFGQVK SVRLVVNIRD
     THAMLLDALS GQQDEYQDLF NDNRITFSEA MAKLYQRINP HIDMGQRTAQ TIGEELLDYR
     NYLELEVEVF RGADGWLRAE SGALSTGEAI GTGMSILLMV VQSWEEESRR IRGKDIVPCR
     LLFLDEAARL DGKSISTLFE LCERLDMQLL IAAPENISPE KGTTYKLVRK IAGNQEYVHV
     VGLRGFGATE