ID   MUKB_ACTPJ              Reviewed;        1496 AA.
AC   B0BUD9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=APJL_0574;
OS   Actinobacillus pleuropneumoniae serotype 3 (strain JL03).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=434271;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JL03;
RX   PubMed=18197260; DOI=10.1371/journal.pone.0001450;
RA   Xu Z., Zhou Y., Li L., Zhou R., Xiao S., Wan Y., Zhang S., Wang K., Li W.,
RA   Li L., Jin H., Kang M., Dalai B., Li T., Liu L., Cheng Y., Zhang L., Xu T.,
RA   Zheng H., Pu S., Wang B., Gu W., Zhang X.L., Zhu G.-F., Wang S.,
RA   Zhao G.-P., Chen H.;
RT   "Genome biology of Actinobacillus pleuropneumoniae JL03, an isolate of
RT   serotype 3 prevalent in China.";
RL   PLoS ONE 3:E1450-E1450(2008).
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; CP000687; ABY69144.1; -; Genomic_DNA.
DR   RefSeq; WP_012262865.1; NC_010278.1.
DR   AlphaFoldDB; B0BUD9; -.
DR   SMR; B0BUD9; -.
DR   EnsemblBacteria; ABY69144; ABY69144; APJL_0574.
DR   KEGG; apj:APJL_0574; -.
DR   HOGENOM; CLU_004430_0_0_6; -.
DR   OMA; FIAVYQH; -.
DR   OrthoDB; 331846at2; -.
DR   Proteomes; UP000008547; 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..1496
FT                   /note="Chromosome partition protein MukB"
FT                   /id="PRO_1000187465"
FT   REGION          694..811
FT                   /note="Flexible hinge"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   REGION          1082..1101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          328..493
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          536..632
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          861..1171
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          1235..1291
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   BINDING         63..70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
SQ   SEQUENCE   1496 AA;  170757 MW;  EDF9951BFE9B57E9 CRC64;
     MTDTNELFED QTTALQNSAP IAPLANPQHT VSRGKFRSLT LINWNGFFAR TFDLDELVTT
     LSGGNGAGKS TTMAGFVTAL IPDLTLLNFR NTTEAGSTSS SRDKGLYGKL KAGVCYAVLE
     SLNSRGQRVI TGVRLQQVAG RDKKVDIRSF SLQNVPMSDS IISVLTEQVG EKARVLPLAD
     LKDKFDGSEV VFKQYHSITD YHSFMFDLGV IPKRLRSSAD RSKFYKLIEA SLYGGISSVI
     TKSLRDYLLP ENTGVRQAFQ DMESALRENR MTLEAIKVTQ SDRDMFKRLI TESTNYVSAD
     YMRNANERRG NVQIALEQRR AWYESKSKLE LEQQRLIEFS REVADISENE SSLEAEYNSA
     NDHLNLVMNA LRHQEKIERY QDEVAELNEK LEEQQIALEE VSEQVETAQA RADDADDQVE
     ELRSQMADYQ QALDAQQTRA LQYQQAIAAL EKAKQLCGLP HLDLHNVEDY HAEFAAQADD
     LTDQVFELEQ RLSVSDMAKT QFEKAYELVC KISGEIDRSE AWDEARSLLT AFTDQKMQAT
     QAVALRQKLA DLEQRLHQQQ NAERLLAEFN QKAQTQFETA EELEGYFEQQ QARLEDVEAE
     LAEFVEVRST QRQQREQLNQ QYNQLAKTAP AWHTAQSALA RLEEQCGEKF EASQSVMQFM
     QNMLTKEREA TLARDKLARR EAALDAQITR LSQPDGSDDV RLNQLAERFG GVLLSELYDD
     VSIDDAPYFS ALYGEARHAI VVRDLESVKS QLEKLDDCPT DLYLIEGDPS AFDDAVFTAE
     ELAEGVVVKV SDRQWRYSKF PEVPLFGRAA REKHLETLKA ERDEVSEQHA ERAFDVQKCQ
     RLHQHLSQFV GTHLSLAFQP NPEEQMQEIA AERTEIEREL NQAAGNEQQL RSQLDSAKAK
     LQMLNKILPL VSLLEDETLA DRAEECRAQL DEAEEDEQFV RQFGNYLTQL EPIAASLKSD
     PAKFEQLEQD YRQAKAEQKQ VQQKVFALSD VIQRRVHFSY EEAIGSEGSA LTEQLRTRLE
     NAQREREQAR DQLRQAQAQF TQYNQVLTGL RSSCDAKTQM LQELIREIDD LGVRGDIGAE
     ERARSRRDEL QQRLSQQRSR KGYLDKQLGT IEAEIDNLTR TLRKAERDYH TQRELVVQAK
     VSWCLVLKLS RNSDVEKRLN RRELAYQSAE ELRSISDKAL GALRTAVADN EYLRDSLRAS
     EDSRKPENKV AFFIAVYQHL RERIRQDIIK TDDPIDAIEQ MEIELSRLTN ELTSREKKLA
     ISAESVANIL RKTIQREQNR ILQLNQGLQN IAFGQVKGVR LVVNIRDTHA ILLNALSNGR
     EEHKDLFDSQ KLSFSEALAM LYKRVNPHIE MGQRTPQTIG EELLDYRNYL DLEVETFRGA
     DGWMRAESSA LSTGEAIGTG MSILLMVVQS WEEESRRMRA KDILPSRLLF LDEAARLDAT
     SINTLFELCE RLDMQLLIAA PENISPERGT TYKLVRKITN NQEYVHVVGL KGFGQQ