MUKB_GLAP5
ID MUKB_GLAP5 Reviewed; 1496 AA.
AC B8F3Q0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=HAPS_0263;
OS Glaesserella parasuis serovar 5 (strain SH0165) (Haemophilus parasuis).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Glaesserella.
OX NCBI_TaxID=557723;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH0165;
RX PubMed=19074396; DOI=10.1128/jb.01682-08;
RA Yue M., Yang F., Yang J., Bei W., Cai X., Chen L., Dong J., Zhou R.,
RA Jin M., Jin Q., Chen H.;
RT "Complete genome sequence of Haemophilus parasuis SH0165.";
RL J. Bacteriol. 191:1359-1360(2009).
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; CP001321; ACL31952.1; -; Genomic_DNA.
DR RefSeq; WP_012621638.1; NC_011852.1.
DR AlphaFoldDB; B8F3Q0; -.
DR SMR; B8F3Q0; -.
DR STRING; 557723.HAPS_0263; -.
DR EnsemblBacteria; ACL31952; ACL31952; HAPS_0263.
DR KEGG; hap:HAPS_0263; -.
DR PATRIC; fig|557723.8.peg.270; -.
DR HOGENOM; CLU_004430_0_0_6; -.
DR OMA; FIAVYQH; -.
DR Proteomes; UP000006743; 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;
KW Reference proteome.
FT CHAIN 1..1496
FT /note="Chromosome partition protein MukB"
FT /id="PRO_1000187479"
FT REGION 694..811
FT /note="Flexible hinge"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 326..492
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 534..632
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 863..942
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 1005..1171
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 1235..1291
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT BINDING 62..69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
SQ SEQUENCE 1496 AA; 171744 MW; 8FA763645FD2EBCD CRC64;
MTEKNDLFEQ NVTSQNIMVA THVQSSIPSV SRSKFRSLTL INWNGFFART FDLDELVTTL
SGGNGAGKST TMAGFVTALI PDLTLLNFRN TTEAGSTSSS RDKGLYGKLK AGVCYAVLES
ENSRGQRVIS GVRLQQIAGR DKKVDIRSFS LQNINENQSV ISILTEQVGE KNARVLALND
LKEKFDGSEV QFKQYHSITD YHSFLFDLGV IPKRLRTSGD RSKFYKLIEA SLYGGISSVI
TKSLRDYLLP ENTGVRQAFQ DMESALRENR MTLEAIKVTQ SDRDMFKKLI TESTNYVSAD
YMRHANERRG NVQQAIEKRQ EWYQSKSKLT LEQQRLVEFS REMQDLEQGE SSLEAEYNSA
SDHLNLVMNA VRHQEKVERY QDDVAELNER LEEQQMALEE VAERQEMAQA RATEAEDQVE
ELRSQMADYQ QALDAQQTRA LQYQQAVNAL EKAKQISGLA NLDLHNVEDY HAEFVAQADE
ITDKVFELEQ RLSVSDMAKS QFDKAYELVC KIAGETDRLQ ADSVARELLS AYPSQKAHAQ
QAVALRQKLT ELEQRLHQQQ NAERLLAEFN QKAQAELENA EDLESYYEEQ QARLEDLEAE
LAEFVEVRST QRQQREQLNQ QYQQLAQTAP AWHTAQSALA RLQEQCGETF DSSQAVMQFM
QNTLSREREA TLERDELARR EQLLDEQISR LSQPDGAEDI RLNQLAEKFG GVLISELYED
VSIEDAPYFS ALYGDARHAI VVRNLEAVKA QLQQLDDCPE NLYLIEGDPN AFDDNVFKSE
ELGDGVVVQL SDRQWRYSKF SEFAVFGRAS REKQLEKVKA ERDETTEKHA ERAFDVQKCQ
RLHQHLSQFV GTHLALAFQP DPEVAMQEIA QKRAEIEREL NQASGTEQQL RHQLENSKAQ
LQLLNKVLPQ LNILADETLQ DRVEECREQL LEAQEDEQFI RQFGNALAQL EPIAVALKSD
PTQFEQLQAD YKRSVEQQKL QQQKVFALAD VMNRRLHFSY QETVGAEGSA LNEQLRQRLD
NAQREREQAR EQLRQATAQF SEYNQVLTSL RSAFDAKNQM LQELLQEMDE YGIRNDDGAE
ERARIRRDEL QQRLSQHRMR KSYIDKQVAV IQAEMDNLNK AVRKAERDYH TQREIVVQAK
VSWCLVLKLS RNSDVEKRLN RRELAYQSAE ELRSISDKAL GALRTAVADN EYLRDSLRAS
EDSRKPENKV VFFILVYQHL RERIRQDIIK TDDPIDAIEQ MEIELSRLTN ELTSREKKLA
ISSESVANIL RKTIQREQNR ILQLNQGLQN IAFGQVKGVR LVVNIRDTHA ILLNALSNDR
EQHSDLFENQ KLSFSEALAM LYKRVNPHIE LGQRTPQTIG EELLDYRNYL DLEVETFRGA
DGWMRAESSA LSTGEAIGTG MSILLMVVQS WEEESRRMRA KDILPARLLF LDEAARLDAT
SINTLFELCE RLDMQLLIAA PENISPERGT TYKLVRKITN NQEYVHVVGL KGFGRV