MUKB_KLEP7
ID MUKB_KLEP7 Reviewed; 1482 AA.
AC A6T716;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=KPN78578_09260; ORFNames=KPN_00951;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) 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; CP000647; ABR76387.1; -; Genomic_DNA.
DR RefSeq; WP_012068512.1; NC_009648.1.
DR AlphaFoldDB; A6T716; -.
DR SMR; A6T716; -.
DR STRING; 272620.KPN_00951; -.
DR jPOST; A6T716; -.
DR EnsemblBacteria; ABR76387; ABR76387; KPN_00951.
DR KEGG; kpn:KPN_00951; -.
DR HOGENOM; CLU_004430_0_0_6; -.
DR OMA; FIAVYQH; -.
DR Proteomes; UP000000265; 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..1482
FT /note="Chromosome partition protein MukB"
FT /id="PRO_1000069910"
FT REGION 666..783
FT /note="Flexible hinge"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 326..472
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 507..602
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 780..805
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 832..1110
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 1209..1265
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 1482 AA; 169555 MW; 54D4AF621489C3E3 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
QALERAKALC HLPDLTPESA DEWLETFQAK EQEATEKMLS LEQKMSVAQT AHSQFEQAYQ
LVAAINGPLA RNEAWDVARE LLRDGVNQRH QAEQAQGLRS RLNELEQRLR EQQDAERQLA
EFCKRQGKRY DIDDLETLHQ ELEARIASLA DSVSNAQEQR MALRQELEQL QSRTQTLMRR
APVWLAAQNS LNQLCEQSGE QFASGQEVTE YLQQLLERER EAIVERDEVG ARKRAIDEEI
ERLSQPGGSE DPRLNALAER FGGVLLSEIY DDVSLDDAPY FSALYGPSRH AIVVPDLSRV
AEQLEGLEDC PEDLYLIEGD PQSFDDSVFS VDELEKAVVV KIADRQWRYS RFPSLPLFGR
AARENRIETL HAERESLSER FATLSFDVQK TQRLHQAFSR FIGSHLAVAF EDDPEEEIRK
LNSRRGELER ALSAHESDNQ QNRVQYEQAK EGVSALNRLL PRLNLLADDT LADRVDEIQE
RLDEAQEAAR FIQQYGNQLA KLEPIVSVLQ SDPEQFEQLK EDYAYAQQTQ RDARQQAFAL
AEVVQRRAHF SYSDSAEMLS GNSDLNEKLR QRLEQAESER SRARDAMRAH AAQLSQYNQV
LASLKSSYDT KKELLNDLYK ELQDIGVRAD AGAEERARAR RDELHMQLSN NRSRRNQLEK
ALTFCEAEMD NLTRKLRKLE RDYCEMREQV VTAKAGWCAV MRLVKDNGVE RRLHRRELAY
LSADELRSMS DKALGALRLA VADNEHLRDV LRISEDPKRP ERKIQFFVAV YQHLRERIRQ
DIIRTDDPVE AIEQMEIELS RLTEELTNRE QKLAISSRSV ANIIRKTIQR EQNRIRMLNQ
GLQSVSFGQV NSVRLNVNVR ETHSMLLDVL SEQHEQHQDL FNSNRLTFSE ALAKLYQRLN
PQIDMGQRTP QTIGEELLDY RNYLEMEVEV NRGSDGWLRA ESGALSTGEA IGTGMSILVM
VVQSWEDESR RLRGKDISPC RLLFLDEAAR LDARSIATLF ELCERLEMQL IIAAPENISP
EKGTTYKLVR KVFNNHEHVH VVGLRGFAAP LPEALPGTAD AS