MUKB_ERWT9
ID MUKB_ERWT9 Reviewed; 1483 AA.
AC B2VC99;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=ETA_21300;
OS Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS 4357 / Et1/99).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=465817;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99;
RX PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA Geider K.;
RT "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT bacterium in the genus Erwinia.";
RL Environ. Microbiol. 10:2211-2222(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}.
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; CU468135; CAO97176.1; -; Genomic_DNA.
DR RefSeq; WP_012441847.1; NC_010694.1.
DR AlphaFoldDB; B2VC99; -.
DR SMR; B2VC99; -.
DR STRING; 465817.ETA_21300; -.
DR PRIDE; B2VC99; -.
DR EnsemblBacteria; CAO97176; CAO97176; ETA_21300.
DR KEGG; eta:ETA_21300; -.
DR eggNOG; COG3096; Bacteria.
DR HOGENOM; CLU_004430_0_0_6; -.
DR OMA; FIAVYQH; -.
DR OrthoDB; 331846at2; -.
DR Proteomes; UP000001726; 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; 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;
KW Reference proteome.
FT CHAIN 1..1483
FT /note="Chromosome partition protein MukB"
FT /id="PRO_1000187477"
FT REGION 666..783
FT /note="Flexible hinge"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT REGION 850..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 311..426
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 547..607
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 835..1115
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 1206..1266
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
SQ SEQUENCE 1483 AA; 169674 MW; CBD2769528CD9BDC CRC64;
MIERGKFRSL TLINWNGFFA RTFDLDELVT TLSGGNGAGK STTMAAFITA LIPDLTLLHF
RNTTEAGATS GSRDKGLHGK LRPGVCYAAL DVVNSLHQRV IVGVRLQQIA GRDRKVDIKP
FSIHGLPTAI NPTEILTESV SARHARVLPL SELKEKFEAM ESVQFKQYNS ITDYHSVMFD
LGIVARRLRT AADRSKYYRL IEASLYGGIS SAITRSLRDY LLPENGGVRK AFQDMEAALR
ENRMTLEAIR VTQSDRDLFK HLISEATNYV SADYMRHANE RRIHLDAALL LRNELFTSRK
QRASEQYRHI EMARELAEHN AAESDLETDY QGASDHLNLV QTALRQQEKI DRYDADLEEL
TFRLEEQNEV VAEAREVQED NEARSEAAEL EVDELKSQLA DYQQALDVQQ TRAIQYQQAL
QALQRAQDIC QLRDLSVDNA EEWQETFQAK ELEATDKLLM LEQKMSVAQA AHSQFEQAYE
LVTRIAGPVS RSDAWQVGRD VLRDAGNQRY HAEQLEPLRS RVSELGQRLR EQQDAERLLS
DFCKRYGQQV DAADLENLQA ELEAQIELLN ESVADAGERR MTLRQELEQL RERIARLTKQ
APQWLAAQEI LSQLGEQTGQ ALENSQQVTE FMQQLLERER ETTVERDDIA ARKREIERQI
ERLSQPGGSE DARLNHLAER FGGVLLSEIY DDVTIDDAPY FSALYGPARH AIVVPDLSLI
REQLDGLDDC PEDLYLIEGD PQSFDDSVFN VEELAKAVVV KAGDRQWRYS RFPKVPLFGR
AARENQLEVL RAERETLAER FATLSFDVQK IQRLHQSFSR FIGSHIGVAF EPDPEAALRQ
LNGRRNEVER ELNNHESENQ QQRQQYEQAK EGVSQLNRLL PRVSLLLDDT LQDRHEEIQE
RLAEAQEATR FVQQHGAQLA RLEPILAVLQ SDPEQHEQLT LDYQQAQQQQ RDARQQAFAL
TEVVQRRAHF GYIDSAGMLN GTSDLNEKLR QRLEQAEAER ARAREQLRQH QSQLTQYSQV
LASLKSSFDA KRDMLKELQQ EMQDIGVHAD ASAEQRARLR RDELYGALSN NRARRNQLEK
QLTFCEAEMD ALQKKLRRLE RDYQQGREQV VSAKAGWVTV LRMVKDNGVE RRLHRRELAY
LGGDELRSMS DKALGALRLA VADNEHLRDV LRLSEDPKRP ERKIQFYIAV YQHLRERIRQ
DIIRTDDPVE AIEQMEIELN RLTEELTARE QTLAISSRSV SNIIRKTIQR EQNRIRQLNQ
GLQAVSFGQV KSVRLNVNVR EAHSTLLDVL SEQHEQHQDL FKSNRLTFSE ALAKLYQRLN
PQIDMGQRTP QTIGEELLDY RNYLEMEVEV SRGSDGWLRA ESGALSTGEA IGTGMSILVM
VVQSWEEESR RLRGKDISPC RLLFLDEAAR LDAKSIATLF ELCDRLEMQL IIAAPENISP
EKGTTYKLVR KVFNNTEHVH VVGLRGFSAE PGAATGSADV GAH