ID   MUKB_VIBCH              Reviewed;        1491 AA.
AC   Q9KRC8;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=VC_1714;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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; AE003852; AAF94864.1; -; Genomic_DNA.
DR   PIR; D82166; D82166.
DR   RefSeq; NP_231350.1; NC_002505.1.
DR   RefSeq; WP_000572788.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KRC8; -.
DR   SMR; Q9KRC8; -.
DR   STRING; 243277.VC_1714; -.
DR   PRIDE; Q9KRC8; -.
DR   DNASU; 2613719; -.
DR   EnsemblBacteria; AAF94864; AAF94864; VC_1714.
DR   GeneID; 57740366; -.
DR   KEGG; vch:VC_1714; -.
DR   PATRIC; fig|243277.26.peg.1640; -.
DR   eggNOG; COG3096; Bacteria.
DR   HOGENOM; CLU_004430_0_0_6; -.
DR   OMA; FIAVYQH; -.
DR   BioCyc; VCHO:VC1714-MON; -.
DR   Proteomes; UP000000584; 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; 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..1491
FT                   /note="Chromosome partition protein MukB"
FT                   /id="PRO_0000068229"
FT   REGION          667..784
FT                   /note="Flexible hinge"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   REGION          1059..1080
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          302..450
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01800"
FT   COILED          490..600
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..1239
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   1491 AA;  169960 MW;  A515AAC8A761A011 CRC64;
     MIERGKYQSL TMINWNGFFA RTFDIDNLVT TLSGGNGAGK STTMAAFITA LIPDQSLLHF
     RNTTEAGSSQ ASRDKGLYGK LQAGACYAAL DVVNSRNQRL LFAVKLQQVA GRDKKVDIKP
     FLIQGLPSHV KPTDVLVETV SDKHARVRQI NEVKDAVGQI EGAHFKSFPS IVDYHAQMFE
     FGVIPKKLRN SSDRSKFYRL IEASLYGGIS SAITRSLRDY LLPQNGGVKK AFQDMESALR
     ENRMTLEAIK TTQADRDLFK HLITESTNYV AADYMRHAND RRNKVGQTLV LRGELFSSRE
     TLIEQNSLLN RVHEELELLV EQESALEQDY QGASDHLQLV QNALRQQEKI ERYQEDLEEL
     NFRLEEQMMV VEEANERVMQ AEERAIISEE EVDSLKSQLA DYQQALDVQQ TRALQYQQAV
     QALDKARRLL DKSELTAESA QALATQLKAE QETRTSELLA LKHKLDMSSA AAQQFNHAFE
     LVKRVLGEVA RSEAAKQAQQ VIRQAREAQN VVQNEAQWQA QQRDLERQLE QQRSVRELAT
     QYHKQHRVVL DDAATVELER ERHSALLEEL ETEQENCREQ RGQLRHQEQE LQTQIARFES
     IAPAWIKAND ALETLREQSG AELADSQSVM AHMQQVLELE KAQSMAKDKL AERRTKLDSE
     IERLASPGGS NDPRLKGLAD TLGGVLLSEI YDDITIDDAP YFSAMYGPAR HAIVVSDLSG
     IKEKLVELDD CPEDLYLIEG DVDAFDDSSF NAEELEGAVC VQLNQRQMRY SRFPAIPLFG
     RAAREQRLEL LREERDDVVE QHAKASFDSQ KLQRLYASFN QFVAMHLQVA FDADPEQALA
     TARDKRNQLL RSISEFEAQE QQLRSQLQAS KQALAALDKL APQMGLLDEE TLEARYHELE
     EKLQQLSEAK AFIAAHGRTI SELEKVAAVL DADPEQFDAL EQQYQQADQA LQQLKAQIFA
     LSDLLERRHH FAYSDSVDLL NQSSELSEQL KAKLVQAESE RTRSREELKQ AQAQLSQYNQ
     LLASLKSSHQ AKLETVQEFK QELQEFGVHA DEGAIERAQR RRDELQERLH TSRSRKSEYE
     RTITSTELEM KALVKRMKKV EKDYQDLRTF VVNAKAGWCS VLRLARQNDV ERRLHKRELA
     YLSADELRSM SDKSLGALRL AVANNEDLRD ALRQSEDNSR PERKVLFYIA VYQHLRERIR
     QDIIRTDDPV EAIEEMEVEL ARLTEELTQR EQRLAISSDS VASIIRKTIQ REQNRIRMLN
     QGLSNISFGQ VNGVRLNVKV RESHEILLAG LSEQQAQHKD LFESARYTFS EAMAKLFQRV
     NPHIDMGQRS PQVLGEELLD YRNYLELSVE VNRGSDGWLQ AESGALSTGE AIGTGQSILL
     MVVQSWEEES RRLRSKDIVP CRLLFLDEAA RLDAKSIATL FELCERLDMQ LLIAAPENIS
     PEKGTTYKLV RKVFKDHEHV HVVGLRGFAQ TEKPKTAEQK FAEELAGELT E