ID   MUKB_SERP5              Reviewed;        1482 AA.
AC   A8GCI9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, 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}; OrderedLocusNames=Spro_1725;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-2007) 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; CP000826; ABV40829.1; -; Genomic_DNA.
DR   RefSeq; WP_012006152.1; NC_009832.1.
DR   AlphaFoldDB; A8GCI9; -.
DR   SMR; A8GCI9; -.
DR   STRING; 399741.Spro_1725; -.
DR   EnsemblBacteria; ABV40829; ABV40829; Spro_1725.
DR   KEGG; spe:Spro_1725; -.
DR   eggNOG; COG3096; Bacteria.
DR   HOGENOM; CLU_004430_0_0_6; -.
DR   OMA; FIAVYQH; -.
DR   OrthoDB; 331846at2; -.
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..1482
FT                   /note="Chromosome partition protein MukB"
FT                   /id="PRO_1000069911"
FT   REGION          666..783
FT                   /note="Flexible hinge"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          337..468
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          509..604
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          780..805
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          835..1044
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          1070..1115
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          1210..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;  169494 MW;  A30CEB5343D181B2 CRC64;
     MIERGKFRSL TLVNWNGFFA RTFDLDELVT TLSGGNGAGK STTMAAFVTA LIPDLTLLHF
     RNTTEAGATS GSRDKGLHGK LRAGVCYSTL DVLNSRHQRV VVGVRLQQVA GRDRKVDIKP
     FVIQGLPTAV QPTELLTQTV GERQARVLSL QELKDRVEEM EGVQFKQFNS ITDYHSLMFD
     LGVIPKRLRS SSDRSKFYRL IEASLYGGIS SAITRSLRDY LLPENSGVRK AFQDMEAALR
     ENRMTLEAIR VTQSDRDLFK HLISEATSYV AADYMRHANE RRIHLDGALA LRNDLLGSRK
     QLAAEQYRHV EMARELAEQS GAESDLETDY QAASDHLNLV QTAMRQQEKI ERYEGDLEEL
     TYRLEEQNEV VAEASEQQAE NEARAEAAEL EVDELKSQLA DYQQALDVQQ TRAIQYQQAL
     QALDRARTLC QLPELTAENA EHWLDTFQAR EQEATEALLM LEQKLSVADA AHGQFEQAYQ
     LVGKIAGQVS RSEAWQCARE LLRDWPSQQH LAERVQPLRM RLSELEQRLR SQQDAERLLQ
     EFCKRHGQQY QPDELDALQQ ELEERLESLS QGVSDAGERR MEMRQELEQI QQRIRELTTR
     APIWLAAQDA LSQLGEQSGE ALESSQQVTE YMQQLLERER ETTVERDEVA AGKRAVEAQI
     ERLSQPGGAE DQRLVTLAER FGGVLLSEIY DDVTIDDAPY FSALYGPSRH AIVVPDLSLV
     REMLEGLEDC PEDLYLIEGD PQSFDDSVFA VEEQDRAVLV KTAERQWRYS RYPAVPLFGR
     AARENRLEIL HAEREKLAER YATLSFDVQK TQRSHQAFSR FIGNHLAVAF DADPEAEIRG
     LNTRRGEIER ALNNHEAQNQ QQRQQYDQAK EGISALNRLT PLVSLLNDET LQDRVEEIRE
     ELEEAQDAAR HIQQHGVSLT KLEPLLSVLQ SDPQQHEQLQ QDYTQAQSVQ RQAKQQAFAL
     IEVVQRRAHF SYTDSAGMQN ANNDLNDKLR QRLEHAEAER TRAREQLRQY QTQFTQYSQV
     LASLKSSYDA KRDMLKELSQ ELVDIGVQAD ANAEARARTR RDELHAGLST NRARRNQLEK
     QLTFCEAEMD SLQKKLRKLE RDYYQLREQV VTAKAGWCAV MRLVKDNGVE RRLHRRELAY
     MDGDELRSMS DKALGALRLA VSDNEHLRDV LRLSEDPKRP ERKIQFYIAV YQHLRERIRQ
     DIIRTDDPVE AIEQMEIELG RLTEELTARE QKLAISSKSV ANIIRKTIQR EQNRIRMLNQ
     GLQAVSFGQV KSVRLNVNVR EAHATLLDVL SEQQEQHQDL FNSNRLTFSE ALAKLYQRLN
     PQIDMGQRTP QTIGEELLDY RNYLELEVEV FRGSDGWLRA ESGALSTGEA IGTGMSILVM
     VVQSWEEESR RLRGKDISPC RLLFLDEAAR LDAKSIATLF ELCDRLEMQL IIAAPENISP
     EKGTTYKLVR KVFQNHEHVH VVGLRGFANE PPVLGVTAAE TP