MUKB_KLEPN
ID MUKB_KLEPN Reviewed; 1479 AA.
AC Q937H2;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 78.
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 Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
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; AJ417691; CAD10421.1; -; Genomic_DNA.
DR AlphaFoldDB; Q937H2; -.
DR SMR; Q937H2; -.
DR PRIDE; Q937H2; -.
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..1479
FT /note="Chromosome partition protein MukB"
FT /id="PRO_0000068221"
FT REGION 665..782
FT /note="Flexible hinge"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 138..163
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 331..664
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 831..1112
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 1206..1257
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 1479 AA; 169866 MW; D4B5C866BDFAEDE2 CRC64;
MIERGKFRSL TLVNWNGFFA RTFDLDELVT TLSGGNGAGK STTMAAFVTA LIPDLTLLHF
RNTTEAGATS GSRDKGLHGK LRAGVCYSVL DVINSRHQRV VVGVRLQQVA GRDRKVDIKP
FAIQGLPTSI LPTQLLTETL NDRQARVVSL NELKDKLEAM EGVQFKQFNS ITEYHSLMFD
LGVVARRLRS ASDRSKYYRL IEASLYGGIS STITRSLRDY LLPENSGVRK AFQDMEAALR
ENRMTLEAIR VTQSDRDLFK HLISEATNYV AADYMRHANE RRIHLDKALE YRRDLFTSRS
QLAAEQYKHV DMARELQEHN GAEGDLEADY QAASDHLNLV QTALRQQEKI ERYEADLDEL
QIRLEEQNEV VAEAVDRQEE NEARAEAAEL EVDELKSQLA DYQQALDVQQ TRAIQYNQAL
QRWSAKALCH LPDLTPESAD EWLETFQAKE QEATEKMLSL EQKMSVANRA HSQFEQAYQL
VAAINGPWRA NEAWDVAREF VRDGVNQRHQ AEQAQGVRSR LNELEQRLRE QQDAERQLAE
FCKRQGKRYD IDDLETLHQE LEARIASLAD SVSNAQEQRM ALRQELEQLQ SRTQTLMRRA
PVWLAAQNSL NQLCEQSGEQ FASGQEVTEY LQQLLERERE AIVERDEVGR RKRAIDEEIE
RLSQPGGSED PRLNALAERF GGVLLSEIYD DVSLDDAPYF SALYGPSRHA IVVPDLSRVA
EQLEGLEDCP EDLYLIEGDP QSFDDSVFSV DELEKAVVVK IADIQWRYSR FPALPLFGRA
ARENRIETLH AERESLSERF GTLSFDVQKT QRLHQAFSRF IEQHLAVTFE DDPEEEIRKL
KQARGELERT VSAHESDNQQ NRVQYEQAKE GVTALNRILP RLNLLADDTL ADRVDEIQER
LDETQEARFI QQYGNELAKL EPIFRCCRAN PEQFEQLKED YAYAQQTQRD ARQQAFALAE
VVQRRAHFSY SDSAEMLSGN SDLNEKLRQR LEQAESERSR ARDAMRAHAA QLSQYNQVLA
SLKSSYDTKK ELLNDLYKEL QDIGVRADAG KKRARARRHE LHMQLSNNRS RRNQLEKALT
FCEAEMDNLT RKLRKLERDY CEMREQVVTA KAGWCAVMRL VKDNGVERRL HRRELAYLSA
DELRSMSDKA LGALRLAVAD NEHLRDVLRI SEDPKRPERK IQFFVAVYQH LRERIRQDII
RTDDPVEAIE QMEIELSRLT EELTNREQKL AISSRSVANI IRKTIQREQN RIRMLNQGLQ
SVSFGQVNSV RLNVNVRETH SMLLDVLSEQ HEQHQDLFNS NRLTFSEALA KLYQRLNPQI
DMGQRTPQTI GEELLDYRNY LEMEVEVNRG SDGWLRAESG ALSTGEAIGT GMSILVMVVQ
SWEDESRRLR GKDISPCRLL FLDEAARLDA RSIATLFELC ERLEMQLIIA APENISPEKG
TTYKLVRKVF NNHEHVHVVG LRGFDAPLPE ALPGTADAS
