ID   MUKB_VIBPA              Reviewed;        1487 AA.
AC   Q87QW2;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=VP1037;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(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; BA000031; BAC59300.1; -; Genomic_DNA.
DR   RefSeq; NP_797416.1; NC_004603.1.
DR   RefSeq; WP_011105766.1; NC_004603.1.
DR   AlphaFoldDB; Q87QW2; -.
DR   SMR; Q87QW2; -.
DR   STRING; 223926.28806024; -.
DR   EnsemblBacteria; BAC59300; BAC59300; BAC59300.
DR   GeneID; 1188541; -.
DR   KEGG; vpa:VP1037; -.
DR   PATRIC; fig|223926.6.peg.983; -.
DR   eggNOG; COG3096; Bacteria.
DR   HOGENOM; CLU_004430_0_0_6; -.
DR   OMA; FIAVYQH; -.
DR   Proteomes; UP000002493; Chromosome 1.
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; 1.
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..1487
FT                   /note="Chromosome partition protein MukB"
FT                   /id="PRO_0000068230"
FT   REGION          667..784
FT                   /note="Flexible hinge"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          297..458
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          506..601
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          637..666
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          781..806
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          836..1109
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          1210..1266
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   1487 AA;  169746 MW;  BB697C58C4189ED8 CRC64;
     MIERGKYQSL TMVNWNGFFA RTFDIDGLVT TLSGGNGAGK STTMAAFITA LIPDQTLLHF
     RNTTEAGSSQ SSRDKGLYGK LQPGACYAAL DVVNSRNQRL LFAVKLQQVA GRDKKVDIKP
     FVIQGLPSHV KPTDILVESV SATQARVRQI NEVKDAIAEF EGVQFKAFSS IVDYHAQMFE
     FGVIPKKLRN SSDRSKFYRL IEASLYGGIS SAITRSLRDY LLPQNGGVKK AFQDMESALR
     ENRMTLEAIK TTQADRDLFK HLITESTNYV AADYMRHAND RRNKLEQTLS LRSELFGSRE
     TLIEQNNLLN RVQEELELLI ESESALEQDY QAASDHLQLV QNALRQQEKI ERYQEDLEEL
     SERLEEQMMV VEEAQERVMM VEEQATVAEE EVDSLKTQLA DYQQALDVQQ TRALQYQQAV
     QALEKAKQLL GDDCLTAESA QALVSELKNK ESESTNALLS VKHKLDMSSA AAEQFETALK
     LVQSIVGQVE RKDAAEQAKI VITKARESQQ IAQNEQQWRA QHRDLERSLN QQRQARELVK
     EYQKQFHVEL TDEITFEQER ERHAMQIETL EMTQEELREQ RSEQRRLEQD AAAEINKLEA
     IAPTWIAAND ALEKLREQSG VDLEDRHAVM SHMQVVLEQE KELSLAKDKL AERRSQLESE
     IERLASPGGS NDPRLKGLAD TLGGVLLSEI YDDITIDDAP YFSAMYGPAR HAIVVSDLSG
     IEEKLVELDD CPEDLYIIEG DIDAFDDSSF DAEELEGAVC VRMNDRQMRY SRFPEIPLFG
     RAAREQRLEL LRNEREEVVE KHAKAAFDSQ KMQRLYQAFN QFVANHIQVA FEADPEQALA
     NVREKRGQIA RVLADLEAKE QQHRSQLQTS KQALSSLDKL APNMALIEDD TLQARFDELE
     EKIAQLSEAK AFLNNHAKAV AELEKIASAL DADPEQFDAL EAEYKAADEQ LQELKKQIFA
     LSDLVERRHY FAYSDSVDLL NQSSELSEQL KAKLVQAEQM RTRSREELKQ AQGQMNQYNQ
     VLASLKSSHQ AKLETVQEFK QELQEFGVNA DEGAEERAIR RRDELHERLH TSRSRKSEYE
     RTITSTELEM KGLAKRLKKV QKEYAELRTF VVAAKAGWCS VLRLARENDV ERRLHKRELA
     YMSADELRSM SDKSLGALRL AVANNDDLRD ALRLSEDNAR PERKVLFYIA VYQHLRERIR
     QDIIRTDDPV EAIEEMEVEL ARLTEELTQR ENRLAISSES VASIIKKTIQ REQNRIRMLN
     QGLSNISFGQ VKGVRLNVKI RESHEVLLHG LSSQQEQHKD LFESPRFTFS EAMAKLFQRV
     NPHIDMGQRS PQVLGEELLD YRNYLELSVE VNRGSDGWLQ AESGALSTGE AIGTGQSILL
     MVVQSWEEES RRLRSKDIIP CRLLFLDEAA RLDAKSISTL FELCDRLDMQ LLIAAPENIS
     PEKGTTYKLV RKVFKDHEHV HVVGLRGFGQ TDKPKSEVQE MIEEFES