MUKB_YERP3
ID MUKB_YERP3 Reviewed; 1485 AA.
AC A7FJV2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=YpsIP31758_2565;
OS Yersinia pseudotuberculosis serotype O:1b (strain IP 31758).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP 31758;
RX PubMed=17784789; DOI=10.1371/journal.pgen.0030142;
RA Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G.,
RA Fayolle C., Lindler L.E., Carniel E., Ravel J.;
RT "The complete genome sequence of Yersinia pseudotuberculosis IP31758, the
RT causative agent of Far East scarlet-like fever.";
RL PLoS Genet. 3:1508-1523(2007).
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; CP000720; ABS46671.1; -; Genomic_DNA.
DR RefSeq; WP_012105376.1; NC_009708.1.
DR AlphaFoldDB; A7FJV2; -.
DR SMR; A7FJV2; -.
DR EnsemblBacteria; ABS46671; ABS46671; YpsIP31758_2565.
DR KEGG; ypi:YpsIP31758_2565; -.
DR HOGENOM; CLU_004430_0_0_6; -.
DR OMA; FIAVYQH; -.
DR Proteomes; UP000002412; 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.
FT CHAIN 1..1485
FT /note="Chromosome partition protein MukB"
FT /id="PRO_1000069918"
FT REGION 666..783
FT /note="Flexible hinge"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 337..480
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 509..605
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 780..805
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 835..915
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 977..1116
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 1210..1235
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 1485 AA; 169861 MW; B3EC7E1CF11583A7 CRC64;
MIERGKFRSL TLVNWNGFFA RTFDLDELVT TLSGGNGAGK STTMAAFVTA LIPDLTLLHF
RNTTEAGATS GSRDKGLHGK LRAGVCYSTL DVVNSRHQRV VVGVRLQQVA GRDRKVDIKP
FTIQGLPTAI QPTEILTELV AERQARVLSL PELKERVEAM EGVQFKQFNS ITDYHSLMFD
LGVIPKRLRS SADRSKFYRL IEASLYGGIS SAITRSLRDY LLPENSGVRK AFQDMEAALR
ENRMTLEAIR VTQSDRDLFK HLISEATSYV AADYMRHANE RRIHLDSALV LRRDLFSSRK
QLVTEQYRHV EMSRELAEQS GAESDLETDY QAASDHLNLV QTAMRQQEKI ERYQSDLEEL
TYRLEEQSEV VSEASEQQAD NEARAEAAEL EVDELKSQLA DYQQALDVQQ TRAIQYQQAL
QALERARALC QLPELTADNA EEWLETFHAK EQEATESLLQ LEQKLSVADA AHSQFEQAYQ
LVVNIAGEVS RSEAWQTARE LLRDWPSQQH LAERVQPLRM RLSELEQRLR AQQDAERLLQ
EFCKRQGNAY QPEELEALQR ELESQVEELS LSVSDAGERR MAMRQELEQL KLKIQELTAR
APVWLAAQDA LSQLSEQSGE ALEDSRQVTE YMQQLLERER ETTVERDEIA ASKRAIEAQI
ERLSQPSGAE DARLIALAER FGGVLLSEIY DDVTIDDAPY FSALYGPSRH GIVVPDLSLV
REHLQGLDDC PEDLYLIEGD PQSFDDSVFA VEEHEKAVVV KIADRQWRYS RYPEVPLFGR
AARENRLETL YQERDRLAER YATLSFDVQK TQRTHQAFSR FIGSHLAVAF DADPEAEIRL
LNTRRGEIER ALNAHEDQNQ QQRQQFDQAK EGISALNRLI PLVSLLLDET LADRVEEITE
ELAEAQEAAR YIQQHGVSLT KLEPLLSVLQ SDPQQHEQLQ ESYVLAQNSQ RLAKQQAFAL
TEVVQRRAHF SYTDSAGMLT ENSDLNDKLR QRLEQAEAER TRAREQLRQY QSQFTQYSQV
LASLKSSYDA KRDMLKELSQ ELVDIGVPAD ANAEARARAR RDELHAALST NRSRRNQLEK
QLTFCEAEMD SLQKKLRKLE RDYHQIREQV VNAKAGWCAV MRMVKDNGVE RRLHRRELAY
MDGDELRSMS DKALGALRLA VADNEHLRDV LRLSEDPKRP ERKIQFYIAV YQHLRERIRQ
DIIRTDDPVE AIEQMEIELG RLTEELTARE QKLAISSKSV SNIIRKTIHR EQNRIRMLNQ
GLQAVSFGQV KSVRLNVNVR EAHATLLDVL SEQQEQHQDL FNSNRLTFSE ALAKLYQRLN
PQMDMGQRLP QTIGEELLDY RNYLELEVEV YRGADGWLRA ESGALSTGEA IGTGMSILVM
VVQSWEEESR RLRGKDISPC RLLFLDEAAR LDAKSIATLF ELCERLEMQL IIAAPENISP
EKGTTYKLVR KVFQNHEHVH VVGLRGFANE IPSLPPIAAE LQQGG