MUKB_AGGAC
ID MUKB_AGGAC Reviewed; 1496 AA.
AC Q93IE8;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 83.
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};
OS Aggregatibacter actinomycetemcomitans (Actinobacillus
OS actinomycetemcomitans) (Haemophilus actinomycetemcomitans).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Aggregatibacter.
OX NCBI_TaxID=714;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14660695; DOI=10.1093/molbev/msh023;
RA Cobbe N., Heck M.M.S.;
RT "The evolution of SMC proteins: phylogenetic analysis and structural
RT implications.";
RL Mol. Biol. Evol. 21:332-347(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}.
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DR EMBL; AJ417690; CAD10420.1; -; Genomic_DNA.
DR RefSeq; WP_025298387.1; NZ_CP065604.1.
DR AlphaFoldDB; Q93IE8; -.
DR SMR; Q93IE8; -.
DR STRING; 714.ACT75_00190; -.
DR eggNOG; COG3096; Bacteria.
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.
FT CHAIN 1..1496
FT /note="Chromosome partition protein MukB"
FT /id="PRO_0000068213"
FT REGION 693..810
FT /note="Flexible hinge"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 332..496
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 537..608
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 665..692
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 806..832
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 862..1066
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 1101..1139
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 1235..1290
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT BINDING 61..68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
SQ SEQUENCE 1496 AA; 171557 MW; 057E83CA7DE9094C CRC64;
MTEELSLEND VMYTTAEAAP VIFSQNSGVE RGKFRSLTLI NWNGFFARTF DLDELVTTLS
GGNGAGKSTT MAGFVTALIP DLTLLHFRNT TEAGATSGSR DKGLHGKLRP GVCYAALDTI
NSRHQRIIVG VRLQQVAGRD KKVDLKTFSI QGVELSVNPT ALFTETLNER QARVLTLNEL
KDKVEQSGAQ FKQYHSITDY HGMMFDLGII PKRLRSSSDR SKFYKLIEAS LYGGISSAIT
RSLRDYLLPE NLGVKKAFQD MESALRENRM TLEAIKVTQA DRDLFKHLIT ESTNYVAADY
MRNANERRGN IESALNFRQE WYKAKSEQDL SQHRLVDLSR EAAELAENEK TLEVDHQSAL
DHLNLVLNAL RHQEKISRYQ ENVGELTERL EEQKMVVETA NEQLEESQAQ FEQTEQEVDN
LRSQLADYQQ ALDAQQTRAL QYQQAIQALE KAKTLCGLAD LAVKNVDVYH EEFEAQAEVL
TDKVLELEQK MSISEAAKTQ FDKAYQLVCK IVGDVPRSAA WESAKELLRE YPTQKLQAQQ
TPQLRAKLHE LEQRLNQQQS AVRLLNDFNQ RANLSLETAD ELEEFYGEQE ALIEDLSAEL
SDLVVQRSTF RQKRENLTAL YEENARKAPA WLTAQAALER LQDQSGEQFA DSQGVMNFMQ
AQLVKEREFT MERDQLELQR QQLDEQISRL SQPDGSEDAR LNVLAERFGG VLLSELYDDV
PIEDAPYFSA LYGPARHAIV VRDLNAVKEQ LANLEDCPED LYLIEGDPAA FDDSVLSAQE
LELGVVVQVS DRELRYSKFP EIPLFGRAAR EKHLEELQAK REEVAEHYAQ RAFDVQKCQR
LHEHFSQFVG LHLALAFQDN PEQVMARTNQ QRNEIERELN QFLTGEQQIR IRLDDAKERM
QLLNKLIPQL PLLADDSLTD RIEECREQLD LAEQDELFIR QYGVTLSQLE PIANTLQSDP
ENYEHLKADY EQAIQLQKQV QQKVFALADV VQRKAHFNYA ESVQTETSEL NEQLRARLEQ
MQQQRETQRE QLRQVQAQYA QYNQVLIQLQ SSFNSKNQML QELMQEIGEL GVRADEGAEE
RAKIRRDELY QQLSTNRQCR SYIEKQLTLI ESEAENLTRR IRKAERDYKT QRELVTAAKM
SWCVVLRLSR NSDVEKRLNR RELAYLSADE LRSMSDKALG ALRTAVADNE YLRDALRLSE
DSRKPENKVR FFIAVYQHLR ERIRQDILKT DDPIDAIEQM EIELSRLTEE LTGREQKLAI
SSESVANIMR KTIQREQNRI RMLNQGLQNI AFGQVKSVRL VVNIRDTHAM LLDALSGNQS
DYQDLFTDNR MTFSEAIAKL YQRLNPHIDV GQRTAQTIGE ELLDYRNYLD LEVEVYRGAD
GWLRAESGAL STGEAIGTGM SILLMVVQSW EEESRRIRGK DIVPCRLLFL DEAARLDAKS
ISTLFELCER LDMQLLIAAP ENISPEKGTT YKLVRKISGN HEHVHVVGLR GFGTTE