MUKB_ACTP7
ID MUKB_ACTP7 Reviewed; 1496 AA.
AC B3H108;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=APP7_0625;
OS Actinobacillus pleuropneumoniae serotype 7 (strain AP76).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=537457;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP76;
RA Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N.,
RA Tegetmeyer H., Singh M., Gerlach G.F.;
RT "Genome and proteome analysis of A. pleuropneumoniae serotype 7.";
RL Submitted (JUN-2008) 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; CP001091; ACE61277.1; -; Genomic_DNA.
DR RefSeq; WP_005617078.1; NC_010939.1.
DR AlphaFoldDB; B3H108; -.
DR SMR; B3H108; -.
DR EnsemblBacteria; ACE61277; ACE61277; APP7_0625.
DR KEGG; apa:APP7_0625; -.
DR HOGENOM; CLU_004430_0_0_6; -.
DR OMA; FIAVYQH; -.
DR BioCyc; APLE537457:APP7_RS03185-MON; -.
DR Proteomes; UP000001226; 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_1000187464"
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; 170605 MW; FA3C37027C98D3A7 CRC64;
MTDTNELFED QTTALQNSAP IAPLANPQHT VSRGKFRSLT LINWNGFFAR TFDLDELVTT
LSGGNGAGKS TTMAGFVTAL IPDLTLLNFR NTTEAGSTSS SRDKGLYGKL KAGVCYAVLE
SLNSRGQRVI TGVRLQQVAG RDKKVDIRSF SLQNVPMSDS IISILTEQVG EKARVLPLAD
LKDKFDGSEV LFKQYHSITD YHSFMFDLGV IPKRLRSSAD RSKFYKLIEA SLYGGISSVI
TKSLRDYLLP ENTGVRQAFQ DMESALRENR MTLEAIKVTQ SDRDMFKHLI TESTNYVSAD
YMRNANERRG NVQIALEQRR AWYESKSKLE LEQQRLIEFS REVADISENE SGLEAEYNSA
NDHLNLVMNA LRHQEKIERY QDEVAELNEK LEEQQIALEE VSEQVETAQA RADDADDQVE
ELRSQMADYQ QALDAQQTRA LQYQQAIAAL EKAKQLCGLP HLDLHNVEDY HAEFAAQADD
LTDQVFELEQ RLSVSDMAKT QFEKAYELVC KISGEIDRSG AWNEARSLLT AFTDQKMQAT
QAVALRQKLA DLEQRLHQQQ NAERLLAEFN QKAQTQFETA EELEGYFEQQ QARLEDVEAE
LAEFVEVRST QRQQREQLNQ QYNQLAKTAP AWHTAQSALA RLEEQCGEKF EASQSVMQFM
QNMLIKEREA TLARDELARR EAALDAQITR LSQPDGSDDV RLNQLAERFG GVLLSELYDD
VSIDDAPYFS ALYGEARHAI VVRDLESVKS QLEKLDDCPT DLYLIEGDPS AFDDAVFTAE
ELAEGVVVKV SDRQWRYSKF PEVPLFGRAA REKHLETLKA ERDEVSEQHA ERAFDVQKCQ
RLHQHLSQFV GTHLSLAFQP NPEEQMQEIA AERTEIEREL NQAAGNEQQL RTQLDSAKAK
LQMLNKILPL VSLLEDETLA DRAEECRAQL DEAEEDEQFV RQFGNYLTQL EPIAASLKSD
PAKFEQLEQD YQQAKAEQKQ VQQKVFALSD VIQRRVHFSY EEAIGSEGSA LTEQLRARLE
SAQREREQAR 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