ID   MUKB_PHOLL              Reviewed;        1482 AA.
AC   Q7N6B7;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 113.
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=plu1639;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
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; BX571864; CAE13932.1; -; Genomic_DNA.
DR   RefSeq; WP_011145930.1; NC_005126.1.
DR   AlphaFoldDB; Q7N6B7; -.
DR   SMR; Q7N6B7; -.
DR   STRING; 243265.plu1639; -.
DR   PRIDE; Q7N6B7; -.
DR   EnsemblBacteria; CAE13932; CAE13932; plu1639.
DR   GeneID; 24166987; -.
DR   KEGG; plu:plu1639; -.
DR   eggNOG; COG3096; Bacteria.
DR   HOGENOM; CLU_004430_0_0_6; -.
DR   OMA; FIAVYQH; -.
DR   OrthoDB; 331846at2; -.
DR   BioCyc; PLUM243265:PLU_RS08250-MON; -.
DR   Proteomes; UP000002514; 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_0000068224"
FT   REGION          666..783
FT                   /note="Flexible hinge"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          333..665
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          784..1116
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          1209..1260
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;  169835 MW;  89357D4630BC50D2 CRC64;
     MIERGKFRSL TLVNWNGFFA RTFDLDELVT TLSGGNGAGK STTMAAFVTA LIPDLTLLHF
     RNTTEAGATS GSRDKGLHGK LRAGVCYSTL DVINSRHQRV VVGVRLQQVA GRDRKVDIKP
     FMIQGLPTAM QPTQLLTENV GERQARVLPL NELKDRLDEM EGVQFKQFNS ITDYHALMFD
     LGVIPKRLRS ASDRSKFYRL IEASLYGGIS SAITRSLRDY LLPENSGVRK AFQDMEAALR
     ENRITLEAIR VTQSDRDLFK HLITEATAYV SADYMRHANE RRTYLDQALA LRGELFGSHR
     QLATERYRHV EMARELEEQS GASVDLEADH QAASDHLNLV QTAMRQQEKI DRYQGDLEEL
     SYRLEEQTEV VEEAAELQAE YEARAEAAEQ EVDELKSQLA DYQQALDVQQ TRAIQYQQAL
     QALERARELC RLPDLAADNA EAWLETFQAK EQQATESLLT LEQKLSVADA AHSQFERAYQ
     LVKNMVGEIS RSEAWQSARE LLRDWPSQQH LADRVQPLRM RLAELEQRLT NQQNAEFLLN
     EFCKRQGQQY QAEDLEGLQS ELEARQEALS LSVNESGERR MEMRQALEQL KQKIQSLTAR
     APVWLAAQDT LSQLCEQNGE ALASSNDVTE YMQQLLERER EATVERDEVA AQKRELEKQI
     ERLSQPSGAE DSRMIALAER FGGVLLSEIY DDITIDDAPY FSALYGPARH GIVVPDLSLV
     RSHLETLEDC PEDLYLIEGD PQSFDDSVFN AEEQANAVLV KSSDRQWRYS RYPELPLFGR
     AARENRLEAL NLERDTLAER YATLSFDVQK IQRAHQAFSQ FVGKHLSVAF DTDPEAEIRE
     LRQRHTELER ELSRFEEQTQ QQRQQYTQAK ESLTTLNRLI PQVTLLLDET LIDRVEEIRE
     ELDEAQEAAR FLQQHGSALA KLEPMVAVLQ SDPQQHEQLQ QDYETAKQSQ HQAKQQAFAL
     VEVVQRRAHF SYSDSAGMLS ENADLNDKLR QRLEHAESDR SRAREQLRQQ QAQYSQFNQV
     LASLKSSYET KQDMLKELHQ EMKEIGVRAD ANAEMRARER RDQLHEALSA NRSRVNQLEK
     QIAFCEAEMD SLQKKLRKLE RDYYQIREQV VSAKAGWCAV MRMVKDNGVE RRLHRRELAY
     MEGGALRSMS DKALGALRLA VSDNEHLRDA LRLSEDPKRP ERKIQFFIAV YQHLRERIRQ
     DIIRTDDPVD AIEQMEIELA RLTEELTARE QKLAISSKSV ANIIRKTIQR EQNRIRMLNQ
     GLQAVSFGQV RGVRLNVNVR ESHALLLDVL SEQQEQHQDL FNSQRLTFSE AMAKLYQRLN
     PQVDMGQRLP QTIGEELLDY RNYLELDVEV NRGSDGWLKA ESGALSTGEA IGTGMSILVM
     VVQSWEEESR RLRGKDISPC RLLFLDEAAR LDAKSIATLF ELCERLQMQL IIAAPENISP
     EKGTTYKLVR KVFKNHEHVH VVGLRGFGQD VPATQLISDA TA