MUKB_HAEDU
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 03-AUG-2022, entry version 118.
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=HD_1582;
OS Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC Bacteria; Proteobacteria; 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}.
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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 EnsemblBacteria; AAP96363; AAP96363; HD_1582.
DR KEGG; hdu:HD_1582; -.
DR eggNOG; COG3096; Bacteria.
DR HOGENOM; CLU_004430_0_0_6; -.
DR OMA; FIAVYQH; -.
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: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 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
