ID   MUKB_MANSM              Reviewed;        1499 AA.
AC   Q65TL9;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=MS1084;
OS   Mannheimia succiniciproducens (strain MBEL55E).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Basfia.
OX   NCBI_TaxID=221988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBEL55E;
RX   PubMed=15378067; DOI=10.1038/nbt1010;
RA   Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA   Jeong H., Hur C.G., Kim J.J.;
RT   "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT   succiniciproducens.";
RL   Nat. Biotechnol. 22:1275-1281(2004).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016827; AAU37691.1; -; Genomic_DNA.
DR   RefSeq; WP_011200259.1; NC_006300.1.
DR   AlphaFoldDB; Q65TL9; -.
DR   SMR; Q65TL9; -.
DR   STRING; 221988.MS1084; -.
DR   PRIDE; Q65TL9; -.
DR   EnsemblBacteria; AAU37691; AAU37691; MS1084.
DR   KEGG; msu:MS1084; -.
DR   eggNOG; COG3096; Bacteria.
DR   HOGENOM; CLU_004430_0_0_6; -.
DR   OMA; FIAVYQH; -.
DR   OrthoDB; 331846at2; -.
DR   Proteomes; UP000000607; 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; 1.
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..1499
FT                   /note="Chromosome partition protein MukB"
FT                   /id="PRO_0000068222"
FT   REGION          696..813
FT                   /note="Flexible hinge"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          335..501
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          540..622
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          666..695
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          865..940
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          1007..1053
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          1100..1143
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          1238..1294
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   BINDING         64..71
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
SQ   SEQUENCE   1499 AA;  172208 MW;  749BE709C7619494 CRC64;
     MSEELELESE FLPEEKSETI VPATVLTQSA GIERGKFRSL TLINWNGFFA RTFDLDELVT
     TLSGGNGAGK STTMAGFVTA LIPDLTLLHF RNTTEAGASG GSRDKGLHGK LRPGVCYAVL
     DAVNSRQQRI LAGVRLQQVA GRDKKVDIKT FSIQGLEISQ NPTAVLTETV SQRQARVLSL
     TELKDRIEEQ GAQFKQYHSV ADYHAMMFEL GMIPRRLRSS SDRSKFYKLI EASLYGGISS
     AITKSLRDYL LPENLGVRKA FQDMESALRE NRMTLEAIKM TQSDRDLFKH LITETTNYVA
     SDYMRNANER QGNIETALSF RKEWYAAKSE QDLSQHRLID LSREAAELTE NEKALEIDHQ
     SASDHLNLVL NALRHQERIE RYQEDVNELT EKLEEQKIVV ENANEQLEES QLQFETLETE
     VDQIRGQLAD YQQALDAQQT RALQYQQAIQ ALEKAKALCG LADLSVKNAE VYHEEFEAQV
     ETLTDRVLQL EQKMSISEAA KTQFDKAYQL VCKIAGEIPR SAAWDSAKEL LREYPTQKLQ
     AQQTPQLRAK LHELEQRYQQ QQSAVKILKD FNQRAGLSLE TADELEDYHA EQEALIENLT
     AEFSEQVETR STLRQKLEQL TALFEEKARS APAWITAKSA LERLTEQSGE QFEDNQDVMN
     FMQAQLEKER EFTMQRDQLE HKRQQLDEQI SRLSQPDGSE DARLNVLAER FGGVLLSELY
     DDVAIEDAPY FSALYGPARH AIVVRDLNAV KEQLAHLDDC PDDLYLIEGD PAAFDDSVHS
     AQELAQGVVV QVSERELRYS KFPEIPLFGR AAREKYLTEL EAERDKIVEQ YAQRAFDVQK
     CQRLHQQFSQ FVGLHLALAF QPDPEQQMRE INQQRNEINR ELTALSTDEQ QLRIKLDNAK
     EQMQLLNKLI PQLNVIADES LSDKVEECRE QLDIAEQDEI FIRQHGMTLS QLEPIANTLQ
     SDPENYERLK DDLYQAIDMQ KQAQQKAFAL ADVIHRQAHF SYEDTVKTET NDLNEKLRVR
     LEQVQAKREQ QRDQVRQKQQ QFAQYNQVYI QLQSSFETKN QMLKELMDEV GELGLTVDEN
     SEQRARVRKD ELHHQLSTSR QRRSFVEKQL TLIESEAENL TRRIRKAERD YKQQRELVVA
     AKVSWCVVLR LSRNSDVEKR LTRREFAYLS ADELRSMSDK ALGSLRTAVA DNEYLRDALR
     ISEDSRKPEN KVRFFIAVYQ HLRERIRQDI IKTDDPIDAI EQMEIELSRL TDELTGREQK
     LAISSESVAN IMRKTIQREQ NRIRMLNQGL QNISFGQVKS VRLVVNIRDT HAMLLDALSG
     NQEEYQDLFN DNRMTFSEAI AKLYQRLNPH IDMGQRTAQT IGEELLDYRN YLDLQVEVYR
     GADGWLQAES GALSTGEAIG TGMSILLMVV QSWEEESRRI RGKDIIPCRL LFLDEAARLD
     GKSISTLFEL CERLDMQLLI AAPENISPEK GTTYKLVRKI SGNQEHVHVV GLRGFGAKE