ID MUKB_HAEDU Reviewed; 1503 AA. AC Q7VL96; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 123. 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}; GN OrderedLocusNames=HD_1582; OS Haemophilus ducreyi (strain 35000HP / ATCC 700724). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=233412; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=35000HP / ATCC 700724; RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L., RA Nguyen D., Wang J., Forst C., Hood L.; RT "The complete genome sequence of Haemophilus ducreyi."; RL Submitted (JUN-2003) 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}. 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; AE017143; AAP96363.1; -; Genomic_DNA. DR RefSeq; WP_010945395.1; NC_002940.2. DR PDB; 3EUJ; X-ray; 3.10 A; A=33-271, A=1263-1496. DR PDB; 3EUK; X-ray; 4.00 A; A/C/F/H=33-271, A/C/F/H=1263-1496. DR PDBsum; 3EUJ; -. DR PDBsum; 3EUK; -. DR AlphaFoldDB; Q7VL96; -. DR SMR; Q7VL96; -. DR IntAct; Q7VL96; 2. DR STRING; 233412.HD_1582; -. DR KEGG; hdu:HD_1582; -. DR eggNOG; COG3096; Bacteria. DR HOGENOM; CLU_004430_0_0_6; -. DR OrthoDB; 6722439at2; -. DR EvolutionaryTrace; Q7VL96; -. DR Proteomes; UP000001022; 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: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; 1.20.58.850; -; 1. DR Gene3D; 3.40.1140.10; -; 2. DR Gene3D; 1.20.5.420; Immunoglobulin FC, subunit C; 1. DR Gene3D; 3.30.70.3500; MukB, hinge domain; 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 PANTHER; PTHR42963; CHROMOSOME PARTITION PROTEIN MUKB; 1. DR PANTHER; PTHR42963:SF1; CHROMOSOME PARTITION PROTEIN MUKB; 1. DR Pfam; PF04310; MukB; 1. DR Pfam; PF16330; MukB_hinge; 1. DR Pfam; PF13558; SbcC_Walker_B; 1. DR PIRSF; PIRSF005246; MukB; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell cycle; Cell division; Chromosome partition; KW Coiled coil; Cytoplasm; DNA condensation; DNA-binding; Nucleotide-binding; KW Reference proteome. FT CHAIN 1..1503 FT /note="Chromosome partition protein MukB" FT /id="PRO_0000068219" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 696..813 FT /note="Flexible hinge" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800" FT COILED 370..495 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800" FT COILED 536..616 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800" FT COILED 662..697 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800" FT COILED 865..1173 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800" FT COILED 1238..1293 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800" FT BINDING 65..72 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800" FT STRAND 37..46 FT /evidence="ECO:0007829|PDB:3EUJ" FT STRAND 49..55 FT /evidence="ECO:0007829|PDB:3EUJ" FT STRAND 58..64 FT /evidence="ECO:0007829|PDB:3EUJ" FT HELIX 71..82 FT /evidence="ECO:0007829|PDB:3EUJ" FT TURN 86..88 FT /evidence="ECO:0007829|PDB:3EUJ" FT HELIX 109..111 FT /evidence="ECO:0007829|PDB:3EUJ" FT STRAND 114..124 FT /evidence="ECO:0007829|PDB:3EUJ" FT STRAND 130..139 FT /evidence="ECO:0007829|PDB:3EUJ" FT STRAND 143..145 FT /evidence="ECO:0007829|PDB:3EUJ" FT STRAND 151..156 FT /evidence="ECO:0007829|PDB:3EUJ" FT STRAND 159..161 FT /evidence="ECO:0007829|PDB:3EUJ" FT HELIX 163..167 FT /evidence="ECO:0007829|PDB:3EUJ" FT STRAND 168..171 FT /evidence="ECO:0007829|PDB:3EUJ" FT STRAND 174..177 FT /evidence="ECO:0007829|PDB:3EUJ" FT HELIX 180..186 FT /evidence="ECO:0007829|PDB:3EUJ" FT TURN 187..189 FT /evidence="ECO:0007829|PDB:3EUJ" FT HELIX 200..209 FT /evidence="ECO:0007829|PDB:3EUJ" FT STRAND 213..215 FT /evidence="ECO:0007829|PDB:3EUJ" FT HELIX 220..234 FT /evidence="ECO:0007829|PDB:3EUJ" FT HELIX 240..244 FT /evidence="ECO:0007829|PDB:3EUJ" FT HELIX 246..248 FT /evidence="ECO:0007829|PDB:3EUJ" FT TURN 255..258 FT /evidence="ECO:0007829|PDB:3EUJ" FT HELIX 259..262 FT /evidence="ECO:0007829|PDB:3EUJ" SQ SEQUENCE 1503 AA; 172403 MW; 5C847ACCAE02F0EC CRC64; MMNTNELFDQ TAVNSSQDKP LNPPFAVAQP ANIARGKFRS LTLINWNGFF ARTFDFDELV TTLSGGNGAG KSTTMAGFVT ALIPDLTLLN FRNTTEAGST SSSRDKGLYG KLKAGVCYAV LETVNSRAQR IITGVRLQQI AGRDKKVDIR PFSLQNVPMA DSVISLFTEQ VANKARVLSL NDLKEKFEET AVTFKPYHSI TDYHSFMFDL GILPKRLRSS SDRNKFYKLI EASLYGGISS VITKSLRDYL LPENSGVRQA FQDMEAALRE NRMTLEAIKV TQSDRDMFKH LITEATQYVS ADYMRNANER RGNVVSALAQ RRTWYDTKAK LLVEEQRLIE FSREVADINL TEQSLESEYN VANDHLNLVM NALRHQEKII RYQDEVDALN EKLEQQQIAL EEVSEQVEDA QAHTDEIDDR VDGLRSQIAD YQQALDAQQT RALQYQQAIT ALQKAQQLCA LPHLDLDNLK DYQTEFEAQA QDITDHVFEL EQRLSISDMT KTQFEKAYQL VCKVSGEIDR SQAWSEATQL LATFPDQKMQ AAQAVALRQK LADLEQRLHQ QQKVQRLIAE FNQQAAKKLT DFTALENHFE QQQIKLEDLE AELANVIELR SVHRQQQEQL TQQYNQLAKT APAWHTARSV LTRLEEQCAE QFENSQAIMH CMQEMLRKER EATLERDELA RTEAALASQI SQLSQADGAE DIRLNQLAER LGGVLLSELY DDVSLQDAPY FSALYGEARH AIVVRDLTSV KAQLEKLTDC PNDLYLIEGD PTAFDDTVFS AEELYDSVIV KVSNRQWRYS KFPEVPLFGR AAREKHLITL KTERDDIAEQ HAESAFNVQK YQRLHQHLSQ FVGTHLNIAF QPDPEMLMQE IALERQEIEG QLNQAVENEH YLRQQADHLK AELQMLNKIL PLANTLADET VMERFEECRE QLQSAEENEL FVRQFGQYLT QLAPIATSLQ TDPSKFEQLE HDYQQAKSTQ RILQQKVFAL SDVMQRRLHF NYSEENQCEG SALTEQLRTD LALAQQEREQ ARQRLRQAQA QFTQYNQVLI SLRSAYDAKY QMLQELMQEI DDLGVRGDSA AEECARLRRD ELQQQLSQQR ARKGYLDKQL GIIEAEIDNL NRLLRKTERD YQTQRELVVQ AKASWCLVQK LSRNSDVEKR LNRRELAYQS AEELRSISDK ALGALRTAVA DNEYLRDSLR ASEDSRKPEN KVAFFIAVYQ HLRERIRQDI IRTDDPIDAI EQMEIELSRL INELTSREKK LAISAESVAN ILRKTIQREQ NRILQLNQGL QNIAFGQVKG VRLVVNIRDT HSILLNALSD QHEQHKDLFE SQKLSFSEAL AMLYKRVNPH IELGQRMPQT IGEELLDYRN YLDLEVETLR GADGWMRAES SALSTGEAIG TGMSILLMVV QSWEEESRRM RAKDILPCRL LFLDEAARLD AMSINTLFEL CERLDMQLLI AAPENISPEH GTTYKLVRKI LANQEYVHVV GLKGFGQQMN KST //