MUKB_EDWI9
ID MUKB_EDWI9 Reviewed; 1485 AA.
AC C5BAC7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=NT01EI_2437;
OS Edwardsiella ictaluri (strain 93-146).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=634503;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146;
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL Submitted (MAR-2009) 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; CP001600; ACR69607.1; -; Genomic_DNA.
DR RefSeq; WP_015871723.1; NC_012779.2.
DR AlphaFoldDB; C5BAC7; -.
DR SMR; C5BAC7; -.
DR STRING; 67780.B6E78_04330; -.
DR EnsemblBacteria; ACR69607; ACR69607; NT01EI_2437.
DR GeneID; 7959169; -.
DR KEGG; eic:NT01EI_2437; -.
DR PATRIC; fig|634503.3.peg.2160; -.
DR HOGENOM; CLU_004430_0_0_6; -.
DR OMA; FIAVYQH; -.
DR OrthoDB; 331846at2; -.
DR Proteomes; UP000001485; 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..1485
FT /note="Chromosome partition protein MukB"
FT /id="PRO_1000215936"
FT REGION 666..783
FT /note="Flexible hinge"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 311..480
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 519..665
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT COILED 832..1115
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 1485 AA; 168776 MW; F54F7BDAABB73AA8 CRC64;
MIERGKFRSL TLVNWNGFFA RTFDLDELVT TLSGGNGAGK STTMAAFVTA LIPDLTLLHF
RNTTEAGATS GSRDKGLHGK LRPGVCYAAL DVVNSRHQRV LVGVRLQQVA GRDRKVDIKP
FAIQGLPTAY QPTQLLTETV DGRQARVLAL PELKERVEAI DGVQFKQFNS ITDYHALMFD
LGVVPRRLRS AADRSKFYRL IEASLYGGIS SAITRSLRDY LLPENGGVRK AFQDMEAALR
ENRMTLEAIR VTQSDRDLFK HLISEATAYV SADYMRHANE RRSHLDQALQ LRRELLGGRR
QLLSEQYRHV EMARELEEQN GAEADLETDY QAASDHLNLV QTALRQREKI ERYQGDLEEL
SYRLDEQSEV AAEAQEQYES CQERSEAAEA EVDELKSQLA DYQQALDVQQ TRAIQYQQAL
QALARAQTLC TLPALSADDV ESWLEDFRAR EEEATELLLQ LEQKLSVANA AHSQFEEAYR
LVARVVGEVS RSDAWQAGRA LLREWPALQH QAQRVAPIGA RLAELEQRLN AQQDAERLLQ
ECVKRSGRDC DAQQLDALQA ELEAQIDTLT QQAADAGERS MALRQELEQI AGRVGTLSAR
APAWIAAQEA LNALESQCGE TLEESRAVTD QMQQLLERER EYTVERDEIA ARKGALEREI
ERLSQPGGAE DARLIALAER FGGVLLSEIY DDVTLDDAPY FSALYGPSRH AIVVPDLAAV
RAQLAGLEEC PEDLYLIEGD PQSFDDSVFA VEELEKAVVV KIADRQWRYS RFPSLPLFGR
AARESRLETL YTEREALAER YATLSFDVQK IQRLHHAFSR FIGSHLAVVF DNDPEQELRQ
LQQRRGEIER EFTGQDAQTQ QQRQQLQQAR ELAGLLNRLV PQVGLLADET LPDRVDELRE
ELEQARDAAR YLQQHGATLA ALEPVIGVLQ SDPQQHEQLQ QDYQQALQRQ RLTKQQAFAL
TEVAQRRAHF SYSDAVGMLG ENADLNERLR QRLEHAEADR SRSREQLRQH QAQLAQYNQV
LASLKSAFDA KRDMLQELQQ EMQDIGVVAD ASAEARARTR RDELHAALSE NRSRRNQLEK
QITICEAEME SLIKRLRKAE RDYHLMRTQV TQAKAGWCAV MRLVRDNGVE RRLHRRELAY
MDADELRSMS DKALGALRLA VADNEHLRDV LRLSEDPKRP ERKVQFYVAV YQHLRERIRQ
DIIRSDDPID AIEQMEIELA RLTEELTARE QKLAISARSV ANIIRKTIQR EQNRIRMLNQ
GLQSVAFGQV NSVRLNVNVR DSHAMLLNVL SEQQEQHQDL FNSNRLTFSE ALAKLYQRLN
PQIDMGQRTP QTIGEELLDY RSYLEMEVEV NRGSDGWLRA ESGALSTGEA IGTGMSILVM
VVQSWEEESR RLRGKDISPC RLLFLDEAAR LDAKSIATLF ELCERLEMQL IIAAPENISP
EKGTTYKLVR KVFNHIEHVH VVGLRGFSAA AEEEHMAQPL EDTPA